Identification of a GP 64 subdomain involved in receptor binding by 3 budded virions of the baculovirus AcMNPV
نویسنده
چکیده
5 6 7 8 9 10 11 12 Jian Zhou and Gary W. Blissard 13 14 15 16 17 18 19 Boyce Thompson Institute at Cornell University, Ithaca, New York 14853 20 2 Department of Entomology, Cornell University, Ithaca, NY 14853 21 22 23 24 25 26 27 28 29 30 Corresponding Author: 31 Gary W. Blissard 32 Boyce Thompson Institute at Cornell University 33 Tower Road, Ithaca, NY 14853 34 Tel. 607-254-1366 35 Fax: 607-254-1242 36 email [email protected] 37 38 39 40
منابع مشابه
Identification of a GP64 subdomain involved in receptor binding by budded virions of the baculovirus Autographica californica multicapsid nucleopolyhedrovirus.
Enveloped virus entry into host cells is typically initiated by an interaction between a viral envelope glycoprotein and a host cell receptor. For budded virions of the baculovirus Autographa californica multicapsid nucleopolyhedrovirus, the envelope glycoprotein GP64 is involved in host cell receptor binding, and GP64 is sufficient to mediate low-pH-triggered membrane fusion. To better define ...
متن کاملCharacterization of a baculovirus lacking the alkaline nuclease gene.
The Autographa californica multiple nucleocapsid nucleopolyhedrovirus (AcMNPV) alkaline nuclease (AN) associates with the baculovirus single-stranded DNA binding protein LEF-3 and possesses both a 5'-->3' exonuclease and an endonuclease activity. These activities are thought to be involved in DNA recombination and replication. To investigate the role of AN in AcMNPV replication, the lambda Red ...
متن کاملThe GP64 envelope fusion protein is an essential baculovirus protein required for cell-to-cell transmission of infection.
To demonstrate the essential nature of the baculovirus GP64 envelope fusion protein (GP64 EFP) and to further examine the role of this protein in infection, we inactivated the gp64 efp gene of Autographa californica multicapsid nuclear polyhedrosis virus (AcMNPV) and examined the biological properties of this virus in vivo. To provide GP64 EFP during construction of the recombinant GP64 EFP-nul...
متن کاملDisplay of heterologous proteins on gp64null baculovirus virions and enhanced budding mediated by a vesicular stomatitis virus G-stem construct.
The Autographa californica multicapsid nucleopolyhedrovirus (AcMNPV) GP64 envelope glycoprotein is essential for virus entry and plays an important role in virion budding. An AcMNPV construct that contains a deletion of the gp64 gene is unable to propagate infection from cell to cell, and this defect results from both a severe reduction in the production of budded virions and the absence of GP6...
متن کاملAc23, an envelope fusion protein homolog in the baculovirus Autographa californica multicapsid nucleopolyhedrovirus, is a viral pathogenicity factor.
Viral envelope fusion proteins are important structural proteins that mediate viral entry and may affect or determine the host range of a virus. The acquisition, exchange, and evolution of such envelope proteins may dramatically affect the success and evolutionary divergence of viruses. In the family Baculoviridae, two very different envelope fusion proteins have been identified. Budded virions...
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