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Human cytomegalovirus glycoprotein-receptor interactions
L Rasmussen1, S Resta, T Merigan
1Division of Infectious Diseases, Stanford University School of Medicine, California.
Transplantation Proceedings
|June 1, 1991
Summary
Human cytomegalovirus (HCMV) glycoprotein 86 (gH) interacts with a 92 kDa protein on cell surfaces, indicating cellular factors beyond attachment influence viral replication. HCMV glycoprotein 130/55 (gB homologue) binds to a distinct 31 kDa protein.
Area of Science:
- Virology
- Cell Biology
- Molecular Biology
Background:
- Human cytomegalovirus (HCMV) is a significant human pathogen.
- HCMV entry into host cells is mediated by viral envelope glycoproteins.
- Understanding HCMV-host cell interactions is crucial for developing antiviral strategies.
Purpose of the Study:
- To identify and characterize cellular receptors for HCMV envelope glycoproteins.
- To investigate the role of cellular proteins in HCMV infection.
- To determine if cellular receptor presence correlates with HCMV permissiveness.
Main Methods:
- Extraction of proteins from HEL fibroblasts.
- Analysis of glycoprotein-protein interactions using binding assays.
- Characterization of HCMV envelope glycoproteins (gp86 and gp130/55).
Main Results:
- HCMV glycoprotein 86 (gH) binds to a 92 kDa cellular protein (HCMV-gp86 receptor).
- This receptor is present on both HCMV-permissive and non-permissive cells.
- HCMV glycoprotein 130/55 (gB homologue) binds to a 31 kDa protein, with minor interactions at other molecular weights.
- HCMV-gp86 does not bind to the primary HCMV gp130/55 receptor.
Conclusions:
- Cellular factors, in addition to viral attachment, likely regulate HCMV intracellular replication.
- The HCMV-gp86 receptor is broadly distributed, suggesting a role in initial viral interactions.
- Distinct cellular proteins mediate interactions with different HCMV envelope glycoproteins.