ArticleVirology2006
Mapping the conformational epitope of a neutralizing antibody (AcV1) directed against the AcMNPV GP64 protein.
Article in Virology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
34 citing papers in PubMed, 56 citations in OpenAlex.
- Essential histidine residues in Bombyx mori nucleopolyhedrovirus GP64 mediate pH-dependent membrane fusion.Microbiology spectrum · 2025Article
- Deep mutational scanning of rabies glycoprotein defines mutational constraint and antibody-escape mutations.Cell host & microbe · 2025Article
- Resolving viral structural complexity by super-resolution microscopy.Archives of virology · 2024Review
- EXTL3 and NPC1 are mammalian host factors for Autographa californica multiple nucleopolyhedrovirus infection.Nature communications · 2024Article
- Structural transition of GP64 triggered by a pH-sensitive multi-histidine switch.Nature communications · 2024Article
- Conformational Changes in Herpes Simplex Virus Glycoprotein C.Journal of virology · 2022Article
- Identification of Cellular Genes Involved in Baculovirus GP64 Trafficking to the Plasma Membrane.Journal of virology · 2022Article
- Fusogenic Hybrid Extracellular Vesicles with PD-1 Membrane Proteins for the Cytosolic Delivery of Cargos.Cancers · 2022Article
- Critical Residues and Contacts within Domain IV of Autographa californica Multiple Nucleopolyhedrovirus GP64 Contribute to Its Refolding during Membrane Fusion.Journal of virology · 2020Article
- Article
- Improving Baculovirus Transduction of Mammalian Cells by Incorporation of Thogotovirus Glycoproteins.Virologica Sinica · 2019Article
- Acidic pH Mediates Changes in Antigenic and Oligomeric Conformation of Herpes Simplex Virus gB and Is a Determinant of Cell-Specific Entry.Journal of virology · 2018Article
- Characterization of two monoclonal antibodies, 38F10 and 44D11, against the major envelope fusion protein of Helicoverpa armigera nucleopolyhedrovirus.Virologica Sinica · 2016Article
- Herpesvirus Entry into Host Cells Mediated by Endosomal Low pH.Traffic (Copenhagen, Denmark) · 2016Review
- A Betabaculovirus-Encoded gp64 Homolog Codes for a Functional Envelope Fusion Protein.Journal of virology · 2016Article
- Epstein-Barr virus glycoprotein gB and gHgL can mediate fusion and entry in trans, and heat can act as a partial surrogate for gHgL and trigger a conformational change in gB.Journal of virology · 2014Article
- Unraveling the entry mechanism of baculoviruses and its evolutionary implications.Journal of virology · 2014Article
- Improving promiscuous mammalian cell entry by the baculovirus Autographa californica multiple nuclear polyhedrosis virus.Bioscience reports · 2012Article
- Functional analysis of the Autographa californica multiple nucleopolyhedrovirus GP64 terminal fusion loops and interactions with membranes.Journal of virology · 2012Article
- Glycoprotein B of herpes simplex virus 2 has more than one intracellular conformation and is altered by low pH.Journal of virology · 2012Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The envelope glycoprotein GP64 of Autographa californica nucleopolyhedrovirus (AcMNPV) is necessary and sufficient for the acid-induced membrane fusion activity that is required for fusion of the budded virus (BV) envelope and the endosome membrane during virus entry. Infectivity of the budded virus (BV) is neutralized by AcV1, a monoclonal antibody (MAb) directed against GP64. Prior studies indicated that AcV1 recognizes a conformational epitope and does not inhibit virus attachment to the cell, but instead inhibits entry at a step following virus attachment. We found that AcV1 recognition of GP64 was lost upon exposure of GP64 to low pH (pH 4.5) and restored by returning GP64 to pH 6.2. In addition, the AcV1 epitope was lost upon denaturation of GP64 in SDS, but the AcV1 epitope was restored by refolding the protein in the absence of SDS. Using truncated GP64 proteins expressed in insect cells, we mapped the AcV1 epitope to a 24 amino acid region in the central variable domain of GP64. When sequences within the mapped AcV1 epitope were substituted with a c-Myc epitope and the resulting construct was used to replace wt GP64 in recombinant AcMNPV viruses, the modified GP64 protein appeared to function normally. However, an anti-c-Myc monoclonal antibody did not neutralize infectivity of those viruses. Because binding of the c-Myc MAb to the same site in the GP64 sequence did not result in neutralization, these studies suggest that AcV1 neutralization may result from a specific structural constraint caused by AcV1 binding and not simply by steric hindrance caused by antibody binding at this position in GP64.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.