ArticleJournal of virology2002
Disulfide bond configuration of human cytomegalovirus glycoprotein B.
Article in Journal of virology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 34 citations in OpenAlex.
- Pre-Cambrian origin ofeLife · 2026Article
- A temperature-dependent virus-binding assay reveals the presence of neutralizing antibodies in human cytomegalovirus gB vaccine recipients' sera.The Journal of general virology · 2023Article
- Development of novel vaccines against human cytomegalovirus.Human vaccines & immunotherapeutics · 2019Review
- Novel trimeric human cytomegalovirus glycoprotein B elicits a high-titer neutralizing antibody response.Vaccine · 2018Article
- Crystal Structure of the Human Cytomegalovirus Glycoprotein B.PLoS pathogens · 2015Article
- Article
- Modern biomolecular mass spectrometry and its role in studying virus structure, dynamics, and assembly.Angewandte Chemie (International ed. in English) · 2011Review
- B cell repertoire analysis identifies new antigenic domains on glycoprotein B of human cytomegalovirus which are target of neutralizing antibodies.PLoS pathogens · 2011Article
- Peptide inhibition of human cytomegalovirus infection.Virology journal · 2011Article
- Sustained expression of human cytomegalovirus glycoprotein B (UL55) in the seeds of homozygous rice plants.Molecular biotechnology · 2008Article
- Herpes simplex virus glycoprotein B binds to cell surfaces independently of heparan sulfate and blocks virus entry.Journal of virology · 2005Article
- Antigenic domain 1 is required for oligomerization of human cytomegalovirus glycoprotein B.Journal of virology · 2005Article
- Expression and characterization of a soluble form of tomato spotted wilt virus glycoprotein GN.Journal of virology · 2004Article
- Recombinant modified vaccinia virus Ankara expressing a soluble form of glycoprotein B causes durable immunity and neutralizing antibodies against multiple strains of human cytomegalovirus.Journal of virology · 2004Article
- Human cytomegalovirus elicits a coordinated cellular antiviral response via envelope glycoprotein B.Journal of virology · 2004Article
- Specific inhibition of human cytomegalovirus glycoprotein B-mediated fusion by a novel thiourea small molecule.Journal of virology · 2004Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Glycoprotein B (gB) is the most highly conserved of the envelope glycoproteins of human herpesviruses. The gB protein of human cytomegalovirus (CMV) serves multiple roles in the life cycle of the virus. To investigate structural properties of gB that give rise to its function, we sought to determine the disulfide bond arrangement of gB. To this end, a recombinant form of gB (gB-S) comprising the entire ectodomain of the glycoprotein (amino acids 1 to 750) was constructed and expressed in insect cells. Proteolytic fragmentation and mass spectrometry were performed using purified gB-S, and the five disulfide bonds that link 10 of the 11 highly conserved cysteine residues of gB were mapped. These bonds are C94-C550, C111-C506, C246-C250, C344-C391, and C573-C610. This configuration closely parallels the disulfide bond configuration of herpes simplex type 2 (HSV-2) gB (N. Norais, D. Tang, S. Kaur, S. H. Chamberlain, F. R. Masiarz, R. L. Burke, and F. Markus, J. Virol. 70:7379-7387, 1996). However, despite the high degree of conservation of cysteine residues between CMV gB and HSV-2 gB, the disulfide bond arrangements of the two homologs are not identical. We detected a disulfide bond between the conserved cysteine residue 246 and the nonconserved cysteine residue 250 of CMV gB. We hypothesize that this disulfide bond stabilizes a tight loop in the amino-terminal fragment of CMV gB that does not exist in HSV-2 gB. We predicted that the cysteine residue not found in a disulfide bond of CMV gB, cysteine residue 185, would play a role in dimerization, but a cysteine substitution mutant in cysteine residue 185 showed no apparent defect in the ability to form dimers. These results indicate that gB oligomerization involves additional interactions other than a single disulfide bond. This work represents the second reported disulfide bond structure for a herpesvirus gB homolog, and the discovery that the two structures are not identical underscores the importance of empirically determining structures even for highly conserved proteins.
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