Naturally Occurring Fragments from Two Distinct Regions of the Prostatic Acid Phosphatase Form Amyloidogenic Enhancers of HIV Infection
| Autor: | Jacqueline Schnell, Wolf-Georg Forssmann, Ludger Ständker, Frank Kirchhoff, Christoph Meier, Nadia R. Roan, Onofrio Zirafi, Jan Münch, Franziska Arnold, Tanja Weil, Warner C. Greene, Christina M. Stürzel |
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| Rok vydání: | 2012 |
| Předmět: |
Male
Amyloid Acid Phosphatase Amino Acid Motifs Molecular Sequence Data Immunology Human immunodeficiency virus (HIV) Virus Attachment HIV Infections Semen Peptide Biology medicine.disease_cause Microbiology Cell Line Virology medicine Humans Amino Acid Sequence Vector (molecular biology) Enhancer Hiv transmission chemistry.chemical_classification Molecular biology Peptide Fragments Virus-Cell Interactions Biochemistry Prostatic acid phosphatase chemistry Insect Science HIV-1 Protein Tyrosine Phosphatases Sequence Alignment |
| Zdroj: | Journal of Virology |
| ISSN: | 1098-5514 0022-538X |
| Popis: | Semen is the major vector for HIV-1 transmission. We previously isolated C-proximal fragments of the prostatic acid phosphatase (PAP) from semen which formed amyloid fibrils that potently enhanced HIV infection. Here, we used the same methodology and identified another amyloidogenic peptide. Surprisingly, this peptide is derived from an N-proximal fragment of PAP (PAP85-120) and forms, similar to the C-proximal fragments, positively charged fibrillar structures that increase virion attachment to cells. Our results provide a first example for amyloid formation by fragments of distinct regions of the same precursor and further emphasize the possible importance of amyloidogenic peptides in HIV transmission. |
| Databáze: | OpenAIRE |
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