Suppression of Human Immunodeficiency Virus Type 1 Replication by Arginine Deiminase of Mycoplasma Arginini.
From: Department of Immunotherapeutics, Graduate School, Tokyo Medical and Dental University, 1-5-45 Yushima, Bunkyo-ku, Tokyo 113-8519, Japan.
The Journal of general virology
- Publish Date: Jun 2006
- ISSN: 0022-1317
- Volume: 87
- Issue: Pt 6
- Pages: 1589-93
- Medium: Print
- Language: English
- Citation (JAMA): Kubo Makoto, Nishitsuji Hironori, Kurihara Kiyoshi, et al. Suppression of Human Immunodeficiency Virus Type 1 Replication by Arginine Deiminase of Mycoplasma Arginini.. J. Gen. Virol. Jun 2006;87:1589-93
Abstract
It was found previously that human immunodeficiency virus type 1 (HIV-1)-irrelevant CD8+ cytotoxic T lymphocytes (CTLs) from uninfected donors suppressed HIV-1 replication in a cell-contact-dependent manner. However, one of these CTL lines (CTL-3) also significantly suppressed HIV-1 replication through its supernatant. Here, the suppressive fraction from CTL-3 supernatant was purified and analysed by mass spectrometry. A protein band specific for the suppressive fraction was identified as arginine deiminase from Mycoplasma arginini, which catalyses the hydrolysis of arginine to citrulline. Addition of L-arginine or the use of antibiotics against mycoplasma restored supernatant-mediated but not cell-contact-dependent suppression of HIV-1 replication by CTL-3, clearly indicating that arginine deiminase of M. arginini in the supernatants suppressed HIV-1 replication, which is independent of CD8+ T-cell-mediated HIV-1 suppression via cell contact. Arginine deiminase is known to be a chemotherapeutic agent against arginine-requiring tumours and these results suggest that it also has potential application in antiviral therapy.
Mesh Headings (Keywords): Cells, Cultured, Culture Media, Conditioned, HIV-1, Humans, Hydrolases, Mass Spectrometry, Mycoplasma, T-Lymphocytes, Cytotoxic, Virus Replication
Check for Full Text / PubMed Unique Identifier (PMID): 16690923
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