Antigenic and functional analysis of a neutralization site of HSV-1 glycoprotein D
dc.contributor.author | Muggeridge, Martin I. | en_US |
dc.contributor.author | Wu, Tsung-Teh | en_US |
dc.contributor.author | Johnson, David C. | en_US |
dc.contributor.author | Glorioso, Joseph C. | en_US |
dc.contributor.author | Eisenberg, Roselyn J. | en_US |
dc.contributor.author | Cohen, Gary H. | en_US |
dc.date.accessioned | 2006-04-10T13:50:51Z | |
dc.date.available | 2006-04-10T13:50:51Z | |
dc.date.issued | 1990-02 | en_US |
dc.identifier.citation | Muggeridge, Martin I., Wu, Tsung-Teh, Johnson, David C., Glorioso, Joseph C., Eisenberg, Roselyn J., Cohen, Gary H. (1990/02)."Antigenic and functional analysis of a neutralization site of HSV-1 glycoprotein D." Virology 174(2): 375-387. <http://hdl.handle.net/2027.42/28742> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B6WXR-4BMSNYN-1M/2/e9aa05985bbd7993cb548c9f082571f9 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/28742 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=2154881&dopt=citation | en_US |
dc.description.abstract | Herpes simplex virus glycoprotein D is a component of the virion envelope and appears to be involved in attachment, penetration, and cell fusion. Monoclonal antibodies (MAbs) against this protein can be arranged in groups, on the basis of a number of biological and biochemical properties. Group I antibodies are type-common, have high complement-independent neutralization titers, recognize discontinuous (conformational) epitopes, and block each other in a binding assay. The sum of their epitopes constitutes antigenic site I of gD. Using a panel of neutralization-resistant mutants, we previously found that group I MAbs can be divided into two subgroups, la and Ib, such that mutations selected with la antibodies have little or no effect on binding and neutralization by Ib antibodies, and vice versa. Antigenic site I therefore consists of two parts, la and Ib. We have now identified the point mutations which prevent neutralization. Two Ib MAbs (DL11 and 4S) selected a Ser to Asn change at residue 140; this alteration creates a new N-linked glycosylation site, which is used. A third Ib MAb (D2) selected a Gin to Leu change at 132. The mutation selected by the Ia MAb HD1 (Ser to Asn at residue 216) is identical to that selected by MAb LP2, another la antibody. By using oligonucleotide-directed mutagenesis, we have produced gD genes with combinations of the above mutations. Attempts to recombine these genes into the virus genome were unsuccessful, suggesting that the combinations are lethal. This was confirmed by a complementation assay which measures the ability of gD transiently expressed in transfected Vero cells to rescue the production of infectious virus by the gD-minus mutant F-gD[beta]. | en_US |
dc.format.extent | 2793828 bytes | |
dc.format.extent | 3118 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Elsevier | en_US |
dc.title | Antigenic and functional analysis of a neutralization site of HSV-1 glycoprotein D | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Public Health | en_US |
dc.subject.hlbsecondlevel | Biological Chemistry | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Departments of Microbiology and Immunology and the Unit for Laboratory Animal Medicine, University of Michigan Medical School, Ann Arbor, Michigan 48109, USA | en_US |
dc.contributor.affiliationother | Department of Microbiology, Veterinary Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA | en_US |
dc.contributor.affiliationother | Center for Oral Health Research, School of Dental Medicine, Veterinary Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA | en_US |
dc.contributor.affiliationother | Department of Pathobiology, School of Veterinary Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA | en_US |
dc.contributor.affiliationother | Molecular Virology and Immunology Program, Department of Pathology, McMaster University, Hamilton, Ontario, Canada L8N 3Z5; Molecular Virology and Immunology Program, Department of Pathology, McMaster University, Hamilton, Ontario, Canada L8N 3Z5. | en_US |
dc.contributor.affiliationother | Center for Oral Health Research, School of Dental Medicine, Veterinary Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA; Department of Microbiology, Veterinary Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA. | en_US |
dc.identifier.pmid | 2154881 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/28742/1/0000572.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0042-6822(90)90091-5 | en_US |
dc.identifier.source | Virology | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
Files in this item
Remediation of Harmful Language
The University of Michigan Library aims to describe library materials in a way that respects the people and communities who create, use, and are represented in our collections. Report harmful or offensive language in catalog records, finding aids, or elsewhere in our collections anonymously through our metadata feedback form. More information at Remediation of Harmful Language.
Accessibility
If you are unable to use this file in its current format, please select the Contact Us link and we can modify it to make it more accessible to you.