Epicuticular waxes of Andropogon hallii and A. Scoparius

Leaf waxes of Andropogon hallii and A. scoparius contain hydrocarbons (2%, 2%), esters (4%, 2%), free acids (3%, 4%), free alcohols (1%, 0.2%, major component dotriacontanol) β-diketones (67%, 80%) and hydroxy β-diketones (16%, 5%). β-Diketones of A. hallii consist mainly of tritriacontane-12,14-dione and hentriacontane-12,14-dione (86:8) and of A. scoparius of tritriacontane-12,14-dione and hentriacontane-10,12-dione (67:29). Hydroxy β-diketones of A. hallii are composed mainly of 5-hydroxytritriacontane-12,14-dione and 5-hydroxy-hentriacontane-12,14-dione (90:8); wax of A. scoparius contains only 5-hydroxytritriacontane-12,14-dione. The hydroxyl group of the major hydroxy β-diketone has the R-configuration opposite to that of all previously described hydroxy β-diketones.     

Epicuticular wax of Eragrostis curvula

Epicuticular wax of Eragrostis curvula contains hydrocarbons (6%), esters (13%), acids (3%), alkanols (4%), tritriacontane-12,14-dione (47%), 5(S)-5-hydroxytritriacontane-12,14-dione (14%) as major components. The esters consist of triterpenol esters (42%) as well as alkanol esters. The free alkanols consist principally Of C₁₆C₃₂ components, resembling those of waxes from panicoid, and some other eragrostoid, grasses. Minor components are triterpenols (0.7%), triterpenones (0.5%), triacylglycerols (0.3%), secondary alkanols (0.1%) and 5-oxotritriacontane-12,14-dione (0.1%).     

Solution structure of the Ca2+-Binding EGF3-4 pair from vitamin K-dependent protein S: identification of an unusual fold in EGF3

Vitamin K-dependent protein S is a cofactor of activated protein C, a serine protease that regulates blood coagulation. Deficiency of protein S can cause venous thrombosis. Protein S has four EGF domains in tandem; domains 2-4 bind calcium with high affinity whereas domains 1-2 mediate interaction with activated protein C. We have now solved the solution structure of the EGF3-4 fragment of protein S. The linker between the two domains is similar to what has been observed in other calcium-binding EGF domains where it provides an extended conformation. Interestingly, a disagreement between NOE and RDC data revealed a conformational heterogeneity within EGF3 due to a hinge-like motion around Glu186 in the Cys-Glu-Cys sequence, the only point in the domain where flexibility is allowed. The dominant, bent conformation of EGF3 in the pair has no precedent among calcium-binding EGF domains. It is characterized by a change in the psi angle of Glu186 from 160 degrees +/- 40 degrees , as seen in ten other EGF domains, to approximately 0 degrees +/- 15 degrees . NOESY data suggest that Tyr193, a residue not conserved in other calcium-binding EGF domains (except in the homologue Gas6), induces the unique fold of EGF3. However, SAXS data, obtained on EGF1-4 and EGF2-4, showed a dominant, extended conformation in these fragments. This may be due to a counterproductive domain-domain interaction between EGF2 and EGF4 if EGF3 is in a bent conformation. We speculate that the ability of EGF3 to adopt different conformations may be of functional significance in protein-protein interactions involving protein S.     

Discovery of Novel Plasmodium falciparum Pre-Erythrocytic Antigens for Vaccine Development

Background

Nearly 100% protection against malaria infection can be achieved in humans by immunization with P. falciparum radiation-attenuated sporozoites (RAS). Although it is thought that protection is mediated by T cell and antibody responses, only a few of the many pre-erythrocytic (sporozoite and liver stage) antigens that are targeted by these responses have been identified.

Methodology

Twenty seven P. falciparum pre-erythrocytic antigens were selected using bioinformatics analysis and expression databases and were expressed in a wheat germ cell-free protein expression system. Recombinant proteins were recognized by plasma from RAS-immunized subjects, and 21 induced detectable antibody responses in mice and rabbit and sera from these immunized animals were used to characterize these antigens. All 21 proteins localized to the sporozoite: five localized to the surface, seven localized to the micronemes, cytoplasm, endoplasmic reticulum or nucleus, two localized to the surface and cytoplasm, and seven remain undetermined. PBMC from RAS-immunized volunteers elicited positive ex vivo or cultured ELISpot responses against peptides from 20 of the 21 antigens.

Conclusions

These T cell and antibody responses support our approach of using reagents from RAS-immunized subjects to screen potential vaccine antigens, and have led to the identification of a panel of novel P. falciparum antigens. These results provide evidence to further evaluate these antigens as vaccine candidates.

Trial Registration

ClinicalTrials.gov NCT00870987 ClinicalTrials.gov NCT00392015     

Biotransformation enzyme expression in the nasal epithelium of woodrats

When herbivores come in contact with volatile plant secondary compounds (PSC) that enter the nasal passages the only barrier between the nasal cavity and the brain is the nasal epithelium and the biotransformation enzymes present there. The expression of two biotransformation enzymes Cytochrome P450 2B (CYP2B) and glutathione-S-transferase (GST) was investigated in the nasal epithelia and livers of three populations of woodrats. One population of Neotoma albigula was fed juniper that contains volatile terpenes. Juniper caused upregulation of CYP2B and GST in the nasal epithelium and the expression of CYP2B and GST in the nasal epithelium was correlated to liver expression, showing that the nasal epithelia responds to PSC and the response is similar to the liver. Two populations of Neotoma bryanti were fed creosote that contains less volatile phenolics. The creosote naive animals upregulated CYP2B in their nasal epithelia while the creosote experienced animals upregulated GST. There was no correlation between CYP2B and GST expression in the nasal epithelia and livers of either population. The response of the nasal epithelium to PSC seems to be an evolved response that is PSC and experience dependent.     

Weichselian interstadial pollen stratigraphy from Härjedalen,central Sweden

Weichselian interstadial vegetation history has been studied by means of pollen analysis of organic bearing fine-grained sediments at Dörrsvålen and Brovalltjärnen in a low mountain area in Härjedalen. The composition of the pollen flora suggests treeless vegetation consisting of shrubs and herbs. The interstadial vegetation consisted of Betula nana, Ericaceae, Juniperus and Salix spp. mixed with herbaceous plant communities including Gramineae, Cyperaceae, Caryophyllaceae, Saxifraga, Rumex/Oxyria and Polygonum. Betula and Pinus are represented by long distance-transported pollen. During the interstadial the climatic conditions seem to have been very harsh and continental as (cold) steppe plants reach high frequencies, e.g. Artemisia and Chenopodiaceae. The sediments are thought to have been deposited during an early Weichselian interstadial tentatively correlated with Tärendö in Norrbotten province, northern Sweden, and Odderade in Denmark and north-western Germany. Comparisons are made with other interstadial sites in central and northern Sweden, and in south-eastern Norway.