In this task, you're given a paragraph from the research paper and your task is to generate a suitable title for the research paper based on the given paper. Under 100 words is a good title length.

Q: 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/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. These results suggest that proteins in the GP64 superfamily are class III penetrenes.

A: Virology Journal Proteomics computational analyses suggest that baculovirus GP64 superfamily proteins are class III penetrenes
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Q: Human papillomavirus (HPV) infection is the most common sexually transmitted disease worldwide. HPVs are oncogenic small double-stranded DNA viruses that are the primary causal agent of cervical cancer and other types of cancers, including in the anus, oropharynx, vagina, vulva, and penis. Prophylactic vaccination against HPV is an attractive strategy for preventing cervical cancer and some other types of cancers. However, there are few safe and effective vaccines against HPV infections. Current first-generation commercial HPV vaccines are expensive to produce and deliver. The goal of this study was to develop an alternate potent HPV recombinant L1-based vaccines by producing HPV virus-like particles into a vaccine that is currently used worldwide. Live attenuated measles virus (MV) vaccines have a well-established safety and efficacy record, and recombinant MV (rMV) produced by reverse genetics may be useful for generating candidate HPV vaccines to meet the needs of the developing world. We studied in non-human primate rMV-vectored HPV vaccine in parallel with a classical alum adjuvant recombinant HPV16L1 and 18L1 protein vaccine produced in Pichia pastoris. A combined prime-boost approach using both vaccines was evaluated, as well as immune interference due to pre-existing immunity against the MV. The humoral immune response induced by the MV, Pichia-expressed vaccine, and their combination as priming and boosting approaches was found to elicit HPV16L1 and 18L1 specific total IgG and neutralizing antibody titres. Pre-existing antibodies against measles did not prevent the immune response against HPV16L1 and 18L1.

A: Immunogenicity of next-generation HPV vaccines in non-human primates: Measles-vectored HPV vaccine versus Pichia pastoris recombinant protein vaccine
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Q: The structural and intracellular proteins of the murine hepatitis viruses MHV-JHM and MHV-A59 were studied by tryptic peptide mapping. The results demonstrated that the virions contained three distinct proteins: the two related chains of the E2 complex, the nucleocapsid protein and the heterogeneous E1 complex. Five distinct virus-specific proteins were synthesized by infected cells. Three of the five intracellular proteins contained tryptic-peptides with properties similar to the three structural proteins. Models describing the evolution of the proteins are proposed. Although the pathogenic properties of MHV-JttM and MHV-A59 differ greatly, the tryptic peptide maps of the corresponding proteins of these MHV strMns were remarkably similar. 334 C.W. BOND, K. A~VD~,~SON, and J. L. LEIBOWITZ: at least seven virus-specific RNA species that function as mRNAs (12, 13, 20, 22) . Five of the seven mRNAs have been translated in vitro and coding assignments have been made (13, 20) . Five to nine virus-specific proteins have been identified in cells infected by MHV-JHM, MHV-A59 or MHV-3 (1, 3, 5, 18, 21) . The virus-specific proteins were identified by comparison of immunoprecipitates of infected and mock-infected cell lysates with purified virions by SDS-polyacryIamide gel electrophoresis (SDS-PAGE). STURMAN (26) proposed a model for the structure of MHV-A59. Three structural proteins were described; the nucleocapsid phosphoprotein (N), the transmembrane gtycoprotein (El) and the peplomerie glycoprotein complex (E 2), which consists of two related proteins. SIDDELL (19) analyzed the structural and intracellular proteins of MHV-JHYI by tryptic peptide mapping of ssS-methionine-labeled proteins. The results indicated that six distinct virus-specific proteins were synthesized by infected cells during the acute infection. The virus particles contained four of these proteins. WEiss and LEIBOWITZ (31) demonstrated by molecular hybridization that the genomes of MHV strains JHM and A59 are closely related in sequence. The molecular weights of the MHV-JHM and MHV-A 59 proteins are similar by SDS-PAGE (2, 3), yet the pathogenic properties of these two viruses are strikingly different (15, 17). In this communication we present tryptic peptide maps of MHV-JHM and MHV-A59 proteins.

A:
Archives of Virology Protein Synthesis in Cells Infected by Murine Hepatitis Viruses JHM and A 59: Tryptie Peptide Analysis
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