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Infect Immun . 2012 Feb 21; Marcsisin RA, Campeau SA, Lopez JE, Barbour AG Borrelia hermsii and other relapsing fever (RF) species are noted for their highly-polymorphic surface antigens, the variable major proteins (VMP). Read more: Infect Immun . 2012 Feb 21; Marcsisin RA, Campeau SA, Lopez JE, Barbour AG Borrelia hermsii and other relapsing fever (RF) species are noted for their highly-polymorphic surface antigens, the variable major proteins (VMP). Less is known about other surface proteins of these pathogens in either their vertebrate reservoirs or arthropod vectors See the original post here: Hum Vaccin Immunother . 2012 Mar 1; 8(3): Sizemore D, Warner E, Lawrence J, Thomas LJ, Roland K, Killeen K Preclinical studies evaluating plague vaccine candidates have demonstrated that the F1 and V antigen proteins of Yersinia pestis provide protection against challenge from virulent strains. Live-attenuated ΔphoP/Q Salmonella typhimurium recombinants expressing either F1, V antigen, F1 plus V antigen, or a F1-V fusion from Asd (+) balanced-lethal plasmids were constructed See more here: Scientist III, Downstream Process Assessment (Purification) at Boehringer Ingelheim (Ridgefield, CT)leads, including antibodies, antibody fragments and proteins. The NBE Unit works as cohesive team within a … functional proteins, including cytokines, glycosylated proteins, and extracellular domains of membrane proteins. Read more here: On this basis, we clone activation macrophage membrane protein NP-2 gene, expression and preparation of polyclonal antibodies against recombinant NP-2 protein.First we query related proteins database, select Serial … See original here: On this basis, we clone activation macrophage membrane protein NP-2 gene, expression and preparation of polyclonal antibodies against recombinant NP-2 protein.First we query related proteins database, select Serial … Continued here: Outer membrane proteins of gram-negative bacteria had been proved to be of high immunocompetence to induce strong specific immunoreaction. As the targets for attacking of the immunocytes and antibodies,they can mediate immunoreaction to kill the bacteria more directly,and play an important role in immune protection.Omp 18 and UreB are outer membrane protein of H.pylori,Which encoding gene show highly conservative.But none of the antigens was capable … View original post here: Outer membrane proteins of gram-negative bacteria had been proved to be of high immunocompetence to induce strong specific immunoreaction. As the targets for attacking of the immunocytes and antibodies,they can mediate immunoreaction to kill the bacteria more directly,and play an important role in immune protection.Omp 18 and UreB are outer membrane protein of H.pylori,Which encoding gene show highly conservative.But none of the antigens was capable … View original post here:
Virus Res. 2011 Dec 31; pUL11 is a highly conserved, small, acylated, membrane-associated tegument protein of herpesviruses. It is involved in final envelopment of nascent virions in the cytoplasm, although the precise mechanism is still unknown. By screening of mouse monoclonal antibodies (mAb) raised against purified particles of infectious laryngotracheitis virus (ILTV) of chickens (Veits et al., 2003a), we identified two mAb recognizing the 15kDa UL11 protein (pUL11) of this avian alphaherpesvirus. These mAb permitted detection and precise localization of pUL11 in mature ILT virions, as well as in the cytoplasm of infected chicken cells by Western blot analyses, indirect immunofluorescence tests, and immunoelectron microscopy. For investigation of gene function UL11-deleted ILTV recombinants were generated. Like its homologues in several other alphaherpesviruses, ILTV-pUL11 was shown to be nonessential for productive virus replication. However, compared to wild-type and UL11 rescued ILTV the deletion mutants exhibited significantly reduced virus yields and moderately impaired spread in cell culture. In the absence of pUL11, electron microscopy of infected cells revealed accumulations of tegument proteins with nucleocapsids, and marked distortions of Golgi membranes in the cytoplasm, which obviously inhibited the formation of mature, enveloped virus particles. Taken together, our results demonstrate that pUL11 is relevant for secondary envelopment of ILTV, and confirm functional conservation of this protein in herpesviruses. The now available unique pUL11-specific mAb will help to further analyze this function, which is presumably mediated by physical interactions with other viral gene products, in cultured cells and in the natural animal host of ILTV. See original here:
Virus Res. 2011 Dec 31; pUL11 is a highly conserved, small, acylated, membrane-associated tegument protein of herpesviruses. It is involved in final envelopment of nascent virions in the cytoplasm, although the precise mechanism is still unknown. By screening of mouse monoclonal antibodies (mAb) raised against purified particles of infectious laryngotracheitis virus (ILTV) of chickens (Veits et al., 2003a), we identified two mAb recognizing the 15kDa UL11 protein (pUL11) of this avian alphaherpesvirus. These mAb permitted detection and precise localization of pUL11 in mature ILT virions, as well as in the cytoplasm of infected chicken cells by Western blot analyses, indirect immunofluorescence tests, and immunoelectron microscopy. For investigation of gene function UL11-deleted ILTV recombinants were generated. Like its homologues in several other alphaherpesviruses, ILTV-pUL11 was shown to be nonessential for productive virus replication. However, compared to wild-type and UL11 rescued ILTV the deletion mutants exhibited significantly reduced virus yields and moderately impaired spread in cell culture. In the absence of pUL11, electron microscopy of infected cells revealed accumulations of tegument proteins with nucleocapsids, and marked distortions of Golgi membranes in the cytoplasm, which obviously inhibited the formation of mature, enveloped virus particles. Taken together, our results demonstrate that pUL11 is relevant for secondary envelopment of ILTV, and confirm functional conservation of this protein in herpesviruses. The now available unique pUL11-specific mAb will help to further analyze this function, which is presumably mediated by physical interactions with other viral gene products, in cultured cells and in the natural animal host of ILTV. Go here to read the rest: |
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