| Title |
Two Highly Conserved Cysteine Residues in HPV16 L2 Form an Intramolecular Disulfide Bond and Are Critical for Infectivity in Human Keratinocytes
|
|---|---|
| Published in |
PLOS ONE, February 2009
|
| DOI | 10.1371/journal.pone.0004463 |
| Pubmed ID | |
| Authors |
Samuel K. Campos, Michelle A. Ozbun |
| Abstract |
Minor capsid protein L2 performs an indispensable but uncharacterized role in human papillomavirus infections. A neutralizing B cell epitope has recently been mapped to the N-terminus of HPV16 L2, residues 17-36, and exposure of this region of L2 has been implicated in translocation of incoming virions from the endo/lysosomal compartment to the cellular cytoplasm. Here we examine the redox state of Cys22 and Cys28 two highly conserved cysteines located within this epitope. We also investigate the infectivity of virions containing L2 single and double cysteine point mutants. |
Mendeley readers
The data shown below were compiled from readership statistics for 43 Mendeley readers of this research output. Click here to see the associated Mendeley record.
Geographical breakdown
| Country | Count | As % |
|---|---|---|
| United States | 1 | 2% |
| Germany | 1 | 2% |
| South Africa | 1 | 2% |
| Unknown | 40 | 93% |
Demographic breakdown
| Readers by professional status | Count | As % |
|---|---|---|
| Student > Ph. D. Student | 17 | 40% |
| Researcher | 7 | 16% |
| Student > Bachelor | 3 | 7% |
| Student > Doctoral Student | 2 | 5% |
| Student > Postgraduate | 2 | 5% |
| Other | 6 | 14% |
| Unknown | 6 | 14% |
| Readers by discipline | Count | As % |
|---|---|---|
| Agricultural and Biological Sciences | 25 | 58% |
| Medicine and Dentistry | 4 | 9% |
| Biochemistry, Genetics and Molecular Biology | 3 | 7% |
| Social Sciences | 1 | 2% |
| Immunology and Microbiology | 1 | 2% |
| Other | 2 | 5% |
| Unknown | 7 | 16% |