Molecular phylogeny of siboglinid annelids (a.k.a. pogonophorans): a review

Siboglinid, or pogonophoran, annelids are tubicolous worms that rely on chemoautotrophic endosymbionts for nutrition. Three clades within the siboglinids are recognized: Frenulata, Vestimentifera, and Monilifera. As a group, these worms have received considerable attention from molecular phylogenetists. Most studies have focused either on the evolutionary origins of the group or on the relationships within vestimentiferans, which live at hydrocarbon seeps and hydrothermal vents. Here I review the literature to date on siboglinid molecular phylogeny and summarize the clade’s evolution. The vestimentiferans have been well studied, especially in the eastern Pacific. The seep taxon Lamellibrachia is basal in the clade with vent species being more derived. Recent studies of seeps are finding new species and suggest that habitat depth can be correlated with species boundaries. In contrast to the vestimentiferans, frenulate evolution has been poorly studied. Despite their greater apparent diversity, frenulate specimens have not been sampled so extensively, and thus little is known about their evolution. Sclerolinum, also referred to as Monilifera, is a recognized genus of siboglinids that forms the sister group to Vestimentifera. Like the frenulates, little is known about the history of this group. Our present understanding of siboglinid phylogeny has, in large part, been dictated by insufficient sampling effort.     

On a generalization of a result of W. G. Cochran

A relationship due to W.G. Cochran showing the effect on leastsquares regression coefficients of marginalizing over or conditioningon an explanatory variable is generalized to quantile regressioncoefficients. The condition under which conditioning does notinduce interaction or effect reversal is shown. Examples aregiven. The discussion is simplest when all variables are continuous;the extension to discrete variables is outlined.     

Cationization of protein antigens. VI. Effects of cationization on the immunoregulatory properties of a bovine serum albumin peptide, a.a. 506-589.

Cationization of bovine serum albumin (BSA) causes a profound increase in its immunogenicity. To establish if immunoregulatory properties of an immunosuppressive peptide are affected by cationization, a BSA peptide, a.a. 506-583, was cationized and tested for its immunogenic properties. A greatly reduced amount of cationized peptide compared to native peptide was required to stimulate BSA-primed T cells to proliferate in vitro. Mice primed with the cationized peptide administered with an adjuvant responded with a significantly greater anti-BSA response than mice immunized with the native form of the peptide. In the absence of an adjuvant i.v. or i.p. administration of the native peptide was immunosuppressive, while the cationized form was immunoenhancing. Both forms of the peptide stimulated in vivo induction of L3T4+ (CD4), and Lyt-2+ (CD8) T cells. Removal of Lyt-2+ T cells from lymph node cultures following immunization with the native peptide caused a significant increase in the proliferation of the remaining T cells. This increase was not observed when the mice were immunized with the cationized peptide. No major BSA B cell determinants were present within the peptide sequence. Mice immunized with the peptide exhibited a negligible anti-BSA antibody response compared to those immunized with the whole BSA molecule. Furthermore, the peptide did not inhibit anti-BSA antibody binding to BSA. We demonstrated that cationization modifies immunoregulatory properties of an immunosuppressive BSA-derived peptide.     

Subulatomonas tetraspora nov. gen. nov. sp. is a member of a previously unrecognized major clade of eukaryotes

While a large number of aerobic free-living protists have been described within the last decade, the number of new anaerobic or microaerophilic microbial eukaryotic taxa has lagged behind. Here we describe a microaerophilic genus and species of amoeboflagellate isolated from a near-shore marine site off the coast at Plymouth, Massachusetts: Subulatomonas tetraspora nov. gen. nov. sp. This taxon is closely related to Breviata anathema based on both microscopical features and phylogenetic analyses of sequences of three genes: SSU-rDNA, actin, and alpha-tubulin. However, Subulatomonas tetraspora nov. gen. nov. sp. and B. anathema are morphologically distinctive, differ by 14.9% at their SSU-rDNA locus, and were isolated from marine and 'slightly brackish' environments, respectively. Phylogenetic analyses of these two taxa plus closely related sequences from environmental surveys provide support for a novel clade of eukaryotes that is distinct from the major clades including the Opisthokonta, Excavata, Amoebozoa and 'SAR' (Stramenopile, Alveolate, Rhizaria).     

Gulose as a constituent of a glycoprotein.

The aldohexose gulose was identified as a constituent of a hydroxyproline-rich glycopeptide derived from the glycoprotein SSG 185. This glycoprotein is part of the extracellular matrix of the green alga Volvox carteri. The gulose residue occupies a terminal position in the corresponding saccharide.     

Interruption-deficient mutants of bacteriophage T5. II. Properties of a mutant lacking a specific interruption.

An examination was made of the properties of T5HA4, a mutant of bacteriophage T5 that lacks the single-chain interruption that occurs at 7.9% from the left end of the genome. The DNAs of T5HA4 and the wild type were compared by electrophoresis in agarose gels of both single-stranded fragments produced by denaturation and duplex fragments generated by sequential treatment with exonuclease III and SI nuclease. These studies demonstrated that T5HA4 also lacks an interruption that occurs at 99.6% in wild-type DNA. The interruptions at 7.9 and 99.6% therefore occur within the 8.3% of T5 DNA that is terminally repetitious. Evidence on the location of other interruptions within the terminal repetition was also obtained. Analysis of T5HA4 with a restriction endonuclease indicated that the interruption deficiency is not due to a deletion or addition mutation. The injection of T5HA4 DNA into a host bacterium was found to occur, as with the wild type, in a two-step manner. The interruption at 7.9% is therefore not required for stopping DNA transfer after the initial 8% segment has been injected.