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Tuyển tập báo cáo các nghiên cứu khoa học quốc tế ngành hóa học dành cho các bạn yêu hóa học tham khảo đề tài: Proteomics computational analyses suggest that baculovirus GP64 superfamily proteins are class III penetrenes | Virology Journal BioMed Central Research Proteomics computational analyses suggest that baculovirus GP64 superfamily proteins are class III penetrenes Courtney E Garry1 and Robert F Garry 2 Address Department of Biology The University of Texas at Austin Austin Texas 78701 USA and 2Department of Microbiology and Immunology Tulane University Heath Sciences Center New Orleans Louisiana 70112 USA Email Courtney E Garry-cgarry@mail.utexas.edu Robert F Garry - rfgarry@tulane.edu Corresponding author Open Access Published 18 February 2008 Received I February 2008 Accepted 18 February 2008 Virology journal 2008 5 28 doi 10.1186 1743-422X-5-28 This article is available from http www.virologyj.cOm content 5 1 28 2008 Garry and Garry licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License http creativecommons.org licenses by 2.0 which permits unrestricted use distribution and reproduction in any medium provided the original work is properly cited. Abstract Background 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 .
