Proteomics computational analyses suggest that baculovirus GP64 superfamily proteins are class III penetrenes

dc.creatorGarry, Courtney E.en
dc.creatorGarry, Robert F.en
dc.date.accessioned2014-12-15T17:10:19Zen
dc.date.available2014-12-15T17:10:19Zen
dc.date.issued2008-02-18en
dc.descriptionCourtney E. Garry is with the Department of Biology, The University of Texas at Austin, Austin, Texas, 78701, USA -- Robert F. Garry is with the Department of Microbiology and Immunology, Tulane University Heath Sciences Center, New Orleans, Louisiana, 70112, USAen
dc.description.abstractBackground: Members of the Baculoviridae encode two types of proteins that mediate virus:cell membrane fusion and penetration into the host cell. Alignments of primary amino acid sequences indicate that baculovirus fusion proteins of group I nucleopolyhedroviruses (NPV) form the GP64 superfamily. The structure of these viral penetrenes has not been determined. The GP64 superfamily includes the glycoprotein (GP) encoded by members of the Thogotovirus genus of the Orthomyxoviridae. The entry proteins of other baculoviruses, group II NPV and granuloviruses, are class I penetrenes. -- Results: Class III penetrenes encoded by members of the Rhabdoviridae and Herpesviridae have an internal fusion domain comprised of beta sheets, other beta sheet domains, an extended alpha helical domain, a membrane proximal stem domain and a carboxyl terminal anchor. Similar sequences and structural/functional motifs that characterize class III penetrenes are located collinearly in GP64 of group I baculoviruses and related glycoproteins encoded by thogotoviruses. Structural models based on a prototypic class III penetrene, vesicular stomatitis virus glycoprotein (VSV G), were established for Thogoto virus (THOV) GP and Autographa california multiple NPV (AcMNPV) GP64 demonstrating feasible cysteine linkages. Glycosylation sites in THOV GP and AcMNPV GP64 appear in similar model locations to the two glycosylation sites of VSV G. -- Conclusion: These results suggest that proteins in the GP64 superfamily are class III penetrenes.en
dc.description.catalogingnoterfgarry@tulane.eduen
dc.description.departmentMolecular Biosciencesen
dc.description.sponsorshipen
dc.identifier.Filename1743-422X-5-28en
dc.identifier.citationGarry, Courtney E., and Robert F. Garry. “Proteomics Computational Analyses Suggest That Baculovirus GP64 Superfamily Proteins Are Class III Penetrenes.” Virology Journal 5, no. 1 (February 18, 2008): 28. doi:10.1186/1743-422X-5-28.en
dc.identifier.doidoi:10.1186/1743-422X-5-28en
dc.identifier.urihttp://hdl.handle.net/2152/27861en
dc.language.isoEnglishen
dc.publisherVirology Journalen
dc.rightsAdministrative deposit of works to UT Digital Repository: This works author(s) is or was a University faculty member, student or staff member; this article is already available through open access at http://www.biomedcentral.com. The public license is specified as CC-BY: http://creativecommons.org/licenses/by/4.0/. The library makes the deposit as a matter of fair use (for scholarly, educational, and research purposes), and to preserve the work and further secure public access to the works of the University.en
dc.subjectbaculovirus GP64en
dc.subjectsuperfamily proteinsen
dc.subjectclass III penetrenesen
dc.subjectProteomics computational analysesen
dc.titleProteomics computational analyses suggest that baculovirus GP64 superfamily proteins are class III penetrenesen
dc.typeArticleen

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