ArticleJournal of virology1997
Characterization of a novel third member of the human cytomegalovirus glycoprotein H-glycoprotein L complex.
Article in Journal of virology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed.
- Chemical and biological conjugation strategies for the development of multivalent protein vaccine nanoparticles.Biopolymers · 2023Review
- Identification of functionally important domains of human cytomegalovirus gO that act after trimer binding to receptors.PLoS pathogens · 2022Article
- Review
- The Human Cytomegalovirus UL116 Glycoprotein Is a Chaperone to Control gH-Based Complexes Levels on Virions.Frontiers in microbiology · 2021Article
- Specialization for Cell-Free or Cell-to-Cell Spread of BAC-Cloned Human Cytomegalovirus Strains Is Determined by Factors beyond the UL128-131 and RL13 Loci.Journal of virology · 2020Article
- Polymorphisms in Human Cytomegalovirus Glycoprotein O (gO) Exert Epistatic Influences on Cell-Free and Cell-to-Cell Spread and Antibody Neutralization on gH Epitopes.Journal of virology · 2020Article
- Differential Expression of PDGF Receptor-α in Human Placental Trophoblasts Leads to Different Entry Pathways by Human Cytomegalovirus Strains.Scientific reports · 2020Article
- Review
- Human cytomegalovirus glycoprotein polymorphisms and increasing viral load in AIDS patients.PloS one · 2017Article
- Virion Glycoprotein-Mediated Immune Evasion by Human Cytomegalovirus: a Sticky Virus Makes a Slick Getaway.Microbiology and molecular biology reviews : MMBR · 2016Review
- The contribution of pUL74 to growth of human cytomegalovirus is masked in the presence of RL13 and UL128 expression.The Journal of general virology · 2016Article
- Viral Regulation of Cell Tropism in Human Cytomegalovirus.Journal of virology · 2016Review
- Human Cytomegalovirus gH/gL/gO Promotes the Fusion Step of Entry into All Cell Types, whereas gH/gL/UL128-131 Broadens Virus Tropism through a Distinct Mechanism.Journal of virology · 2015Article
- Human Cytomegalovirus UL135 and UL136 Genes Are Required for Postentry Tropism in Endothelial Cells.Journal of virology · 2015Article
- Principles for studying in vivo attenuation of virus mutants: defining the role of the cytomegalovirus gH/gL/gO complex as a paradigm.Medical microbiology and immunology · 2015Review
- A viral regulator of glycoprotein complexes contributes to human cytomegalovirus cell tropism.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Structural and biochemical studies of HCMV gH/gL/gO and Pentamer reveal mutually exclusive cell entry complexes.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Comparative analysis of gO isoforms reveals that strains of human cytomegalovirus differ in the ratio of gH/gL/gO and gH/gL/UL128-131 in the virion envelope.Journal of virology · 2013Article
- Vaccination with synthetic constructs expressing cytomegalovirus immunogens is highly T cell immunogenic in mice.Human vaccines & immunotherapeutics · 2012Article
- PDGF receptor-α does not promote HCMV entry into epithelial and endothelial cells but increased quantities stimulate entry by an abnormal pathway.PLoS pathogens · 2012Article
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Authors and funding
2 authors.
Funding
Abstract
A prerequisite for understanding the molecular function of the human cytomegalovirus (HCMV) gH (UL75)-gL (UL115) complex is a detailed knowledge of the structure of this complex in its functional form, as it is present in mature virions. The gH protein is known to be a component of a 240-kDa envelope complex designated as gCIII (D. R. Gretch, B. Kari, L. Rasmussen, R. C. Gehrz, and M. F. Stinski, J. Virol. 62:875-881, 1988). However, the exact composition of the gCIII complex remains unknown. In this report, we attempted reconstitution of the gCIII complex by coexpression of gH and gL in the baculovirus expression system. Formation of recombinant gH-gL complexes of approximately 115 kDa was demonstrated; however, no higher-molecular-mass (approximately 240-kDa) recombinant gH-gL complexes were detected, suggesting that the presence of gH and gL alone is not sufficient for reconstitution of the gCIII complex. To identify other mammalian and/or HCMV factors which may be necessary for gCIII formation, immunoprecipitates of gH and gL from HCMV-infected fibroblasts and purified HCMV virions were examined. This analysis did reveal a number of coprecipitating proteins which associate either transiently or integrally with gH and gL. One coprecipitating protein of 145 kDa was shown to be an integral component of gCIII, along with gH and gL. Characterization of the 145-kDa protein demonstrates that it is structurally and antigenically unrelated to gH and gL and that it appears to be virally encoded. Together, these data indicate that the 145-kDa protein is a third novel component of the mature HCMV gH-gL complex.
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