Settlement of Planulae of the Moon Jellyfish Aurelia aurita onto Hydrophilic Polycarbonate Plates Modified by Atmospheric Plasma Treatment

It has been reported that planula larvae of some jellyfish prefer artificial substrates for settlement. This research focused on the relationship between the settlement of planulae and the wettability of artificial substrate surfaces. We used atmospheric plasmas to change the wettability of the surfaces of polycarbonate (PC) plates because plasma treatment has no chemical side effects. The treatment made the surfaces hydrophilic, as evidenced by the decrease of contact angle from 85° to 35°. X-ray photoelectron spectroscopy revealed that the change of wettability of the PC plates could be attributed to N₂, which was probably ionized in the air above the plates. Scanning electron microscopy revealed no difference in the surface morphology of the plates before and after plasma treatment. Results of bioassays using treated PC plates showed that planulae tended to preferentially settle on hydrophobic surfaces.     

Pratylenchus australis n. sp. and Eutylenchus fueguensis n. sp. (Nematoda: Tylenchina) from southern Chile

Two new species of nematodes from southern Chile are described and illustrated. Pratylenchus australis n. sp. is distinguished by its heavy cephalic sclerotization, smooth tail terminus, lack of spermatheca, and absence of males. Eutylenchus fueguensis n. sp. differs from other Eutylenchus spp. by the long female stylet (31 [28-32] μm), strongly sclerotized excretory duct opening posterior to nerve ring, and broadly rounded caudal alae of males.     

Comparative Morphology of Meloidodera spp. and Verutus sp. (Heteroderidae) with Scanning Electron Microscopy

Scanning electron microscopy (SEM) of second-stage juveniles (J2), males, and females of Meloidodera floridensis, M. charis, M. belli, and Verutus volvingentis reveals detailed characteristics of the head region, lateral field, phasmid, body striae, vulva, and perineal region. In M. charis and M. belli the en face pattern conforms to a basic pattern in which the labial disc is surrounded by six lips (sectors) of the first head annulation. In J2 the head has additional annulations, whereas in males annulation is replaced by longitudinal blocks. Conversely, J2 and males of M. floridensis and V. volvingentis each have a unique derived face pattern with fusion of various lip components and with head annulation. All six lips of females of M. charis and M. belli are fused, whereas females of M. floridensis and V. volvingentis have distinct lateral lips. Lateral fields vary among species, with only slight differences at the anterior and posterior ends of the lateral lines and in the spatial relation of the lines to phasmid openings. Phasmid openings are present in adults of Meloidodera spp., but were not observed in adults of V. volvingentis; in this respect, the female perineal pattern of Verutus is different from Meloidodera spp, The very large vulva (± 48 μm long) of V. volvingentis is in sharp contrast to the minute vulva (± 6 μm long) in a population of M. charis from San Bernardino. Morphological characters revealed by SEM will be most informative when investigated throughout Heteroderidae and incorporated with additional characters for a phylogenetic analysis of the family.     

Structural and Functional Analysis of Transmembrane XI of the NHE1 Isoform of the Na+/H+ Exchanger

The Na⁺/H⁺ exchanger isoform 1 is a ubiquitously expressed integral membrane protein that regulates intracellular pH in mammals by extruding an intracellular H⁺ in exchange for one extracellular Na⁺. We characterized structural and functional aspects of the critical transmembrane (TM) segment XI (residues 449-470) by using cysteine scanning mutagenesis and high resolution NMR. Each residue of TM XI was mutated to cysteine in the background of the cysteine-less protein and the sensitivity to water-soluble sulfhydryl reactive compounds MTSET ((2-(trimethylammonium) ethyl)methanethiosulfonate) and MTSES ((2-sulfonatoethyl) methanethiosulfonate) was determined for those residues with at least moderate activity remaining. Of the residues tested, only proteins with mutations L457C, I461C, and L465C were inhibited by MTSET. The activity of the L465C mutant was almost completely eliminated, whereas that of the L457C and I461C mutants was partially affected. The structure of a peptide representing TM XI (residues Lys⁴⁴⁷-Lys⁴⁷²) was determined using high resolution NMR spectroscopy in dodecylphosphocholine micelles. The structure consisted of helical regions between Asp⁴⁴⁷-Tyr⁴⁵⁴ and Phe⁴⁶⁰-Lys⁴⁷¹ at the N and C termini of the peptide, respectively, connected by a region with poorly defined, irregular structure consisting of residues Gly⁴⁵⁵-Gly⁴⁵⁹. TM XI of NHE1 had a structural similarity to TM XI of the Escherichia coli Na⁺/H⁺ exchanger NhaA. The results suggest that TM XI is a discontinuous helix, with residue Leu⁴⁶⁵ contributing to the pore.The mammalian Na⁺/H⁺ exchanger isoform 1 (NHE1)⁴ is a ubiquitous integral membrane protein that regulates intracellular pH. It mediates removal of a single intracellular proton in exchange for an extracellular sodium ion (1). NHE1 has many functions aside from protection of cells from intracellular acidification (2). It promotes cell growth and differentiation (3), regulates sodium fluxes and cell volume after challenge by osmotic shrinkage (4), and has been demonstrated to be involved in modulating cell motility (5). In addition its activity is important in invasiveness of neoplastic breast cancer cells (6). NHE1 also plays critical roles in heart disease. It has a contributing role in heart hypertrophy and in the damage that occurs during ischemia and reperfusion. Inhibition of NHE1 with Na⁺/H⁺ exchanger inhibitors protects the myocardium during various disease states (7-10).NHE1 is composed of two general regions, an N-terminal membrane domain of ∼500 amino acids and a C-terminal regulatory domain of ∼315 amino acids (1, 8). The membrane domain is responsible for ion movement and an analysis of topology by cysteine scanning accessibility suggested it has 3 membrane-associated segments and 12 integral transmembrane segments (11) (Fig. 1A). The mechanism of transport of the membrane domain is of great interest both from a scientific viewpoint and in the design of improved NHE1 inhibitors that may be necessary for clinical use (1). In this regard, we have recently characterized the functionally important residues and the structure of both TM IV and TM VII. Prolines 167 and 168 of TM IV were critical to NHE1 function (12) and cysteine-scanning mutagenesis was used to show that Phe¹⁶¹ is a pore lining residue critical to transport. Analysis of the structure of TM IV showed that TM IV is composed of one region of β-turns, an extended middle region including Pro¹⁶⁷-Pro¹⁶⁸, and a helical region (13). TM VII was much more typical of a transmembrane helix although it was interrupted with a break in the helix at the functionally critical residues Gly²⁶¹-Glu²⁶² (14).Open in a separate windowFIGURE 1.Models of the Na⁺/H⁺ exchanger. A, simplified topological model of the transmembrane domain of the NHE1 isoform of the Na⁺/H⁺ exchanger as described earlier (11). EL, extracellular loop; IL, intracellular loop. B, model of amino acids present in TM XI.Another important TM segment of the Na⁺/H⁺ exchanger is TM XI (Fig. 1B). Several different lines of evidence have suggested that it is critical to NHE1 function. A recent study generated chimeras of NHE1 from various species and found that a region including TM XI was important in determining NHE1 inhibitor sensitivity (15). More specifically, mutagenesis of several amino acids of TM XI has shown that it is likely involved in either ion transport or proper targeting to the plasma membrane. Two mutants in TM XI, Y454C and R458C, are retained in the endoplasmic reticulum (16). In addition, mutation of Gly⁴⁵⁵ and Gly⁴⁵⁶ in TM XI shift the pH_i dependence of the exchanger to the alkaline side, whereas mutation of Arg⁴⁴⁰ in intracellular loop 5 at the N-terminal end of TM XI shifts the pH_i dependence to make it more acidic (17, 18). Also, the structure of the bacterial Na⁺/H⁺ exchanger NhaA has been elucidated. Both TM IV and TM XI play a critical role forming an assembly that cross, with each being a helix, an extended polypeptide and a short helix (19). We found that TM IV of NHE1 has a similar structure and function to that of TM IV of NhaA (2, 13), leaving open the possibility that TM XI of NHE1 is also similar in structure and function to TM XI of NhaA.For these reasons, we undertook a systematic examination of the structural and functional aspects of TM XI of the NHE1 isoform of the Na⁺/H⁺ exchanger. The sequence of human TM XI of NHE1 is ⁴⁴⁹QFIIAYGGLRGAIAFSLGYLLD⁴⁷⁰. In this study we use cysteine scanning mutagenesis and site-specific mutagenesis to identify and characterize critical pore lining residues of the protein. We also use nuclear magnetic resonance (NMR) spectroscopy to characterize the structure of a synthetic peptide representing TM XI in dodecylphosphocholine (DPC) micelles. Evidence has suggested that TM segments of membrane proteins possess all the structural information required to form their higher order structures in their amino acid sequence (20). This has been demonstrated in earlier studies on membrane protein segments such as the cystic fibrosis transmembrane conductance regulator (21), a fungal G-protein-coupled receptor (22), bacteriorhodopsin (23, 24), and rhodopsin (25), where it was shown that isolated TM segments from membrane proteins had structures in good agreement with the segments of the entire protein. Also, the use of DPC micelles has been shown to be an excellent membrane mimetic environment for these studies (26, 27). Our study identifies Leu⁴⁶⁵ as contributing to the pore of the protein and shows that the structure of TM XI consists of two helices corresponding to Asp⁴⁴⁷-Tyr⁴⁵⁴ and Phe⁴⁶⁰-Lys⁴⁷¹ at the N and C termini, respectively, connected by a flexible region at residues 455-459. The structure of TM XI was similar to the x-ray structure of TM XI of NhaA.     

Benzothiadiazole-Mediated Induced Resistance to Fusarium oxysporum f. sp. radicis-lycopersici in Tomato

Benzo-(1,2,3)-thiadiazole-7-carbothioic acid S-methyl ester (BTH), a synthetic chemical, was applied as a foliar spray to tomato (Lycopersicon esculentum) plants and evaluated for its potential to confer increased resistance against the soil-borne pathogen Fusarium oxysporum f. sp. radicis-lycopersici (FORL). In nontreated tomato plants all root tissues were massively colonized by FORL hyphae. Pathogen ingress toward the vascular stele was accompanied by severe host cell alterations, including cell wall breakdown. In BTH-treated plants striking differences in the rate and extent of fungal colonization were observed. Pathogen growth was restricted to the epidermis and the outer cortex, and fungal ingress was apparently halted by the formation of callose-enriched wall appositions at sites of fungal penetration. In addition, aggregated deposits, which frequently established close contact with the invading hyphae, accumulated in densely colonized epidermal cells and filled most intercellular spaces. Upon incubation of sections with gold-complexed laccase for localization of phenolic-like compounds, a slight deposition of gold particles was observed over both the host cell walls and the wall appositions. Labeling was also detected over the walls of fungal cells showing signs of obvious alteration ranging from cytoplasm disorganization to protoplasm retraction. We provide evidence that foliar applications of BTH sensitize susceptible tomato plants to react more rapidly and more efficiently to FORL attack through the formation of protective layers at sites of potential fungal entry.     

Size-based Prey Selectivity and Dietary Shifts in the Jellyfish, Aurelia aurita

Gut content analyses on field-caught Aurelia aurita showed bothquantitative and qualitative change in diet as a function ofmedusa size. Larger medusae tended towards greater numbersand diversity of prey (up to 1550 individual prey representingas many as 13 different prey groups). We also found that medusasize was a good predictor of prey diversity recovered from themedusa gut. While a shift toward greater prey diversity inlarger medusae might be explained by increased contact rateswith 'rare' prey taxa, we also found size-based prey selectivitychanges in A. aurita. We used in situ gut content data to describeselectivity by A. aurita for three prey types representing varyingdegrees of swimming or escape velocity. Fish eggs were usedas a non-swiming prey, and small (     

Structural Basis for the Antiproliferative Activity of the Tob-hCaf1 Complex

The Tob/BTG family is a group of antiproliferative proteins containing two highly homologous regions, Box A and Box B. These proteins all associate with CCR4-associated factor 1 (Caf1), which belongs to the ribonuclease D (RNase D) family of deadenylases and is a component of the CCR4-Not deadenylase complex. Here we determined the crystal structure of the complex of the N-terminal region of Tob and human Caf1 (hCaf1). Tob exhibited a novel fold, whereas hCaf1 most closely resembled the catalytic domain of yeast Pop2 and human poly(A)-specific ribonuclease. Interestingly, the association of hCaf1 was mediated by both Box A and Box B of Tob. Cell growth assays using both wild-type and mutant proteins revealed that deadenylase activity of Caf1 is not critical but complex formation is crucial to cell growth inhibition. Caf1 tethers Tob to the CCR4-Not deadenylase complex, and thereby Tob gathers several factors at its C-terminal region, such as poly(A)-binding proteins, to exert antiproliferative activity.The Tob/BTG family (also called the APRO family) is a group of antiproliferative proteins (1, 2) consisting of Tob (3), Tob2 (4), BTG1 (5), BTG2/Tis21/PC3 (6-8), PC3B (9), and ANA/BTG3 (10, 11) in mammalian cells, {"type":"entrez-nucleotide","attrs":{"text":"AF177464","term_id":"5916227","term_text":"AF177464"}}AF177464 in Drosophila, and FOG-3 in Caenorhabditis elegans (12). A recent genome project reported that the BTG/Tob family protein had already existed in Choanoflagellida Monosiga brevicollis MX1. The N-terminal region of the Tob/BTG family proteins is conserved and includes two highly homologous regions, Box A and Box B. The Tob/BTG family proteins are involved in cell cycle regulation in a variety of cells such as T lymphocytes, fibroblasts, epithelial cells, and germ cells. In Tob-deficient mice, the incidence of liver tumors is higher than in wild-type mice. Furthermore, because the levels of tob expression are often repressed in human lung cancers, suppression of its expression is thought to contribute to tumor progression (13).The antiproliferative activities of the Tob/BTG family proteins are due to their association with target proteins in cells. For example, Tob associates with SMAD family proteins and acts as a negative regulator of SMAD signaling. In osteoblasts, this negative regulation occurs via association with SMAD 1, 5, 6, and 8 (14, 15), and via association with SMAD 2 and 4 in anergic quiescent T cells (16). Tob/BTG family proteins also bind to protein arginine methyltransferase, which regulates chromatin assembly by histone methylation (17). Much evidence has been accumulated to suggest that CCR4-associated factor 1 (Caf1),² also known as Cnot7 and involved in the CCR4-Not deadenylase complex, is a common binding partner of the Tob/BTG family proteins (4, 18-21). To reveal the functions of Caf1 in vivo, caf1^-/- mice have been generated in two groups. Male caf1-deficient mice are infertile because of a malfunction of the testicular somatic cells that leads to a defect in spermatogenesis (22, 23). Genetic analysis of the nematode C. elegans also suggests that FOG3 (Tob orthologue) interacts with CCF1, the C. elegans homologue of Caf1, and that this interaction is essential for germ cells to initiate spermatogenesis (24).Mouse and human Caf1 (mCaf1 and hCaf1) were found as homologues of yeast Pop2, a component of the CCR4-Not complex (18, 25). Yeast Pop2 displays weak RNase activity but enhances the deadenylation of the poly(A) tail of mRNA by the CCR4-Not deadenylase complex (26-29). The primary structure of mammalian Caf1 is related to that of the ribonuclease D (RNase D) family, and all of the active site residues are well conserved (30). Indeed, both mCaf1 and hCaf1 have deadenylase activity (31-33).Although the relationship between cell cycle repression and poly(A) deadenylation is not well understood, mRNA degradation and synthesis are major events in maintaining the cell cycle (34). The mRNAs in a eukaryotic cell have a wide range of half-lives. Degradation of mRNA is initiated by shortening of the poly(A) tail. Thereafter, the 5′-cap structure is removed and the remaining portion of the mRNA is rapidly degraded. The degradation of eukaryotic mRNAs is regulated precisely at each stage of the cell cycle. Tob was reported to associate with inducible poly(A)-binding protein (iPABP) and to abrogate the translation of interleukin-2 mRNA in vitro (35). Recent reports also showed that Tob and BTG2 interact with the CCR4-Not deadenylase complex using the Tob/BTG2 domain and the cytoplasmic poly(A)-binding protein (PABPC1) using the C-terminal tail and enhanced mRNA degradation (36-38).To help elucidate the relationship between the antiproliferative activity of Tob and the degradation of the poly(A) tail, we determined the crystal structure of the Tob-hCaf1 complex. We found that hCaf1 has a structure similar to yeast Pop2 and human PARN of deadenylases, exonuclease I, and the Klenow fragment of DNA polymerase I from Escherichia coli. In contrast, Tob has a novel structure. Specifically, Box A and Box B mediate the interaction between Tob and hCaf1. Cell growth assays using the wild and mutant proteins, together with the structural studies, revealed that the complex formation is crucial to cell growth inhibition.     

Protocylindrocorpus dendrophilus n. sp. (Nematoda: Cylindrocorpidae) Associated with Pine Wood Borings

Protocylindrocorpus dendrophilus n. sp. is described from xylem samples taken from beetle infested slash pine (Pinus elliottii Engelmann var. elliottii) in Central Louisiana. It is similar to P. goodeyi (Rühm) Paramonov, but differs by the possession of a protuberant and more posteriorly located vulva and in the position of the caudal papillae. Morphometrics of the male and female are presented.     

Effect of Starvation on the Endocytic Pathway in Dictyostelium Cells

Dictyostelium discoideum amoebae have been used extensively to study the structure and dynamics of the endocytic pathway. Here, we show that while the general structure of the endocytic pathway is maintained in starved cells, its dynamics rapidly slow down. In addition, analysis of apm3 and lvsB mutants reveals that the functional organization of the endocytic pathway is profoundly modified upon starvation. Indeed, in these mutant cells, some of the defects observed in rich medium persist in starved cells, notably an abnormally slow transfer of endocytosed material between endocytic compartments. Other parameters, such as endocytosis of the fluid phase or the rate of fusion of postlysosomes to the cell surface, vary dramatically upon starvation. Studying the endocytic pathway in starved cells can provide a different perspective, allowing the primary (invariant) defects resulting from specific mutations to be distinguished from their secondary (conditional) consequences.Dictyostelium discoideum is a widely used model organism for studying the organization and function of the endocytic pathway. In Dictyostelium, the organization of the endocytic pathway is similar to that in higher eukaryotes. The pathway in Dictyostelium can be divided into four steps (see Fig. S1 in the supplemental material): uptake at the plasma membrane of particles and medium, transfer through early acidic endocytic compartments (lysosomes), passage into less acidic postlysosomes (PLs), and finally, exocytosis of undigested materials (17, 20). Thus, Dictyostelium recapitulates many of the functions of the endocytic pathway in mammalian cells, including some features observed in most cell types (lysosome biogenesis) and some observed only in specialized cells (phagocytosis, macropinocytosis, and lysosome secretion).Dictyostelium amoebae live in the soil, where they feed by ingesting and digesting other microorganisms. In addition, axenic laboratory strains can macropinocytose medium to ensure their growth. Accordingly, both in natural situations and in laboratory settings, the endocytic pathway plays a key role in the acquisition of nutrients by Dictyostelium cells. In agreement with this notion, several observations suggest that the physiology of the endocytic pathway is sensitive to nutrient availability. In particular, starvation induces secretion of lysosomal enzymes by an unknown mechanism (11). The morphology of the endocytic pathway is also sensitive to nutritional cues, as shown for example by the observation that formation of multilamellar endosomes is enhanced in cells fed with bacteria (18).Here, we analyzed the effect of starvation on the organization as well as the dynamics of the endocytic pathway. We found that, while the overall organization was not extensively modified in starved cells, the dynamics of endocytic compartments were altered. Moreover, analysis of two specific knockout mutants, the apm3 (6) and lvsB (8) strains, revealed that their phenotype was profoundly altered upon starvation, providing further insight about the role of Apm3 and LvsB in the endocytic pathway.     

Descriptions of Chitwoodius brasiliensis n.sp., Chitwoodius rusticulus n.sp., and Vancterlindia venata n.sp. (Dorylaimida: Tylencholaimidae: Vanderlindiinae)

Chitwoodius brasiliensis n.sp. is described from soil around plant roots in Vicosa, MG State, Brazil. It has a body 1.9 mm (1.6-2.5) long, odontostyle and odontophore 33 μm (31-37) and 34 μm (31-36) long, respectively, and males with spicules 59-61 μm long. Chitwoodius rusticulus n.sp. from Colombian rain forest differs from other species of the genus in having a weakly muscular anterior part of the oesophagus, a pore-like vulva, and an unsclerotized vagina. Vanderlindia venata n.sp. from lucerne soil in South Kilimanjaro, Tanzania, differs from the type and only other known species of its genus in having a smaller and less slender body (L = 3.34 mm [3.15-3.71], a = 50 [46-53]), odontostyle 2.3-2.5 times lip region width long, and stylet guiding ring located at 1.2-1.4 times lip region width from anterior end.     

Life Cycle Reversal in Aurelia sp.1 (Cnidaria,Scyphozoa)

The genus Aurelia is one of the major contributors to jellyfish blooms in coastal waters, possibly due in part to hydroclimatic and anthropogenic causes, as well as their highly adaptive reproductive traits. Despite the wide plasticity of cnidarian life cycles, especially those recognized in certain Hydroza species, the known modifications of Aurelia life history were mostly restricted to its polyp stage. In this study, we document the formation of polyps directly from the ectoderm of degenerating juvenile medusae, cell masses from medusa tissue fragments, and subumbrella of living medusae. This is the first evidence for back-transformation of sexually mature medusae into polyps in Aurelia sp.1. The resulting reconstruction of the schematic life cycle of Aurelia reveals the underestimated potential of life cycle reversal in scyphozoan medusae, with possible implications for biological and ecological studies.     

Pratylenchoides hispaniensis n. sp. (Nemata: Pratylenchidae)

Pratylenchoides hispaniensis n. sp. is described and illustrated from a bisexual population found in a natural habitat at Santa Elena, Jaen, central Spain. Its main distinctive characters are very long esophageal gland lobe (81-117 μm; N'' = 51-71) overlapping the intestine 3 to 5 times the body width; lateral field with six incisures; stylet knobs sloping posteriorly; labial disc encircled by the irregular sectors of the first annule; tail cylindrical, extremity annulated, and frequently with a slight dorsal indentation of the hyaline portion at the end of the lateral field. Pratylcnchoides hispaniensis n. sp. appears closely related to P. megalobatus and P. nevadensis. It differs from the former primarily by its longer body length (761-998 vs. 430-621 μm), longer stylet length (20.5-24.4 vs. 18-21 μm), six incisures in the lateral field vs. four for P. megalobatus, and posteriorly sloping stylet knobs vs. rounded or anteriorly flattened knobs in P. megalobatus. It differs from P. nevadensis mainly by the shape of the stylet knobs (sloping in P. hispaniensis vs. rounded in P. nevadensis), length of esophageal lobe (81-117 vs. 34-82 μm), and position of esophageal gland nuclei (all posterior to esophago-intestinal junction in P. hispaniensis vs. at least one nucleus anterior to junction in P. nevadensis).     

Marinobacter salarius sp. nov. and Marinobacter similis sp. nov., Isolated from Sea Water

Two non-pigmented, motile, Gram-negative marine bacteria designated R9SW1^T and A3d10^T were isolated from sea water samples collected from Chazhma Bay, Gulf of Peter the Great, Sea of Japan, Pacific Ocean, Russia and St. Kilda Beach, Port Phillip Bay, the Tasman Sea, Pacific Ocean, respectively. Both organisms were found to grow between 4°C and 40°C, between pH 6 to 9, and are moderately halophilic, tolerating up to 20% (w/v) NaCl. Both strains were found to be able to degrade Tween 40 and 80, but only strain R9SW1^T was found to be able to degrade starch. The major fatty acids were characteristic for the genus Marinobacter including C_16:0, C_16:1 ω7c, C_18:1 ω9c and C_18:1 ω7c. The G+C content of the DNA for strains R9SW1^T and A3d10^T were determined to be 57.1 mol% and 57.6 mol%, respectively. The two new strains share 97.6% of their 16S rRNA gene sequences, with 82.3% similarity in the average nucleotide identity (ANI), 19.8% similarity in the in silico genome-to-genome distance (GGD), 68.1% similarity in the average amino acid identity (AAI) of all conserved protein-coding genes, and 31 of the Karlin''s genomic signature dissimilarity. A phylogenetic analysis showed that R9SW1^T clusters with M. algicola DG893^T sharing 99.40%, and A3d10^T clusters with M. sediminum R65^T sharing 99.53% of 16S rRNA gene sequence similarities. The results of the genomic and polyphasic taxonomic study, including genomic, genetic, phenotypic, chemotaxonomic and phylogenetic analyses based on the 16S rRNA, gyrB and rpoD gene sequence similarities, the analysis of the protein profiles generated using MALDI-TOF mass spectrometry, and DNA-DNA relatedness data, indicated that strains R9SW1^T and A3d10^T represent two novel species of the genus Marinobacter. The names Marinobacter salarius sp. nov., with the type strain R9SW1^T ( =  LMG 27497^T  =  JCM 19399^T  =  CIP 110588^T  =  KMM 7502^T) and Marinobacter similis sp. nov., with the type strain A3d10^T ( =  JCM 19398^T  =  CIP 110589^T  =  KMM 7501^T), are proposed.     

Pseudascarophis brasiliensis sp. nov. (Nematoda: Cystidicolidae) parasitic in the Bermuda chub Kyphosus sectatrix (Perciformes: Kyphosidae) from southeastern Brazil

A new species of Pseudascarophis (Nematoda: Cystidicolidae) found in the stomach of Kyphosus sectatrix (Linnaeus) (Kyphosidae), off Rio de Janeiro, Brazil, is described. The new species can be differentiated from the other congeners by the presence of lateral alae, distinct but inconspicuous cephalic papillae at the anterior end, three pairs of precloacal and one pair of adcloacal papillae in males, egg morphology and morphometry of glandular oesophagus and spicules. Pseudascarophis tropica is transferred to Ascarophis as Ascarophis tropica (Solov''eva) comb. n. due to its ambiguous diagnosis.     

Xiphidorus amazonensis n. sp. (Nematoda: Longidoridae) from the Brazilian Amazon Basin

Xiphidorus amazonensis n. sp. was found in the rhizospheres of Jatropha curcas, Musa sp., Anona muricata, Cassia tora, Panicum laxum, Paspalum fasciculatum, Aeschynomene sensitiva, Saccharum officinarum, Manihot esculenta, Abelmoschus esculentus, Tamarindus indica, Mangifera indica, Vigna unguiculata, Zea mays, Commelina sp., Cyperus rotundus, Fimbristylis miliacea, Citrus sinensis, and Eichhornia crassipes on the Amazon River island of Xiborena, approximately 40 km southeast of Manaus, capital of the State of Amazonas. The type habitat is flooded annually for about 6 months by the Amazon River. Xiphidorus amazonensis n. sp. differs from the closely related species Xiphidorus yepesara Monteiro, 1976 by the larger size, by a, b, and c values, and by the rounded tail terminus. It also resembles Xiphidorus tucumanensis Chaves and Coomans, 1984, but can be distinguished by its larger size, larger a, b, and c values, more conical female tail, bilobed amphidial pouch, and the presence of a spermatheca full of sperm.     

Discocriconemella inaratus n. sp. and Criconemoides inusitatus n. sp. (Nematoda) from Iowa

Discocriconemella inaratus n. sp. from Iowa prairies is characterized by a single offset disk-shaped head annule which is often discontinuous, a sigmoid vagina, a stylet length of 51-61 μm, and 77-100 smooth body annules. Criconemoides inusitatus n. sp. from Iowa woodlands is characterized by two offset head annules, a "closed" vulva, a straight vagina, no overlapping anterior vulva lip, a stylet length of 42-50 μm, and 71-86 smooth body annules.