Two Highly Conserved Cysteine Residues in HPV16 L2 Form an Intramolecular Disulfide Bond and Are Critical for Infectivity in Human Keratinocytes
2009
HPV16 L2 Protein's Critical Role in Infection
publication
Evidence: high
Author Information
Author(s): Samuel K. Campos, Michelle A. Ozbun
Primary Institution: The University of New Mexico School of Medicine
Hypothesis
The cysteine residues C22 and C28 in the HPV16 L2 protein form an intramolecular disulfide bond that is critical for the infectivity of the virus.
Conclusion
The C22 and C28 cysteine residues in HPV16 L2 are essential for the virus's infectivity, as mutations at these sites result in non-infectious virions.
Supporting Evidence
- C22 and C28 cysteines are conserved across papillomaviruses.
- Mutant L2 proteins were degraded more rapidly than wild type L2 during infection.
- All L2 cysteine mutant virions were non-infectious despite normal cell binding and trafficking.
Takeaway
The HPV virus needs certain parts of its proteins to work properly, and if those parts are changed, the virus can't infect cells.
Methodology
The study used gel analysis, thiol labeling experiments, and mass spectrometry to investigate the role of cysteine residues in HPV16 L2.
Digital Object Identifier (DOI)
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