有哪些信誉好的足球投注网站a single amino acid of human immunodeficiency virus type 2 capsid protein affects conformation of two external loops and viral sensitivity to trim5α一个氨基酸的人类免疫缺陷病毒2型衣壳蛋白构象的影响两个外部循环和病毒trim5α敏感性.pdfVIP
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a single amino acid of human immunodeficiency virus type 2 capsid protein affects conformation of two external loops and viral sensitivity to trim5α一个氨基酸的人类免疫缺陷病毒2型衣壳蛋白构象的影响两个外部循环和病毒trim5α敏感性
A Single Amino Acid of Human Immunodeficiency Virus Type 2 Capsid Protein Affects Conformation of Two External Loops and Viral Sensitivity to TRIM5a 1 2 1,3 1 2 Tadashi Miyamoto , Masaru Yokoyama , Ken Kono , Tatsuo Shioda , Hironori Sato , Emi E. Nakayama1* 1 Department of Viral infections, Research Institute for Microbial Diseases, Osaka University, Suita, Osaka, Japan, 2 Pathogen Genomics Center, National Institute of Infectious Diseases, Musashi Murayama, Tokyo, Japan, 3 Research Fellow of the Japan Society for the Promotion of Science, Tokyo, Japan Abstract We previously reported that human immunodeficiency virus type 2 (HIV-2) carrying alanine or glutamine but not proline at position 120 of the capsid protein (CA) could grow in the presence of anti-viral factor TRIM5a of cynomolgus monkey (CM). To elucidate details of the interaction between the CA and TRIM5a, we generated mutant HIV-2 viruses, each carrying one of the remaining 17 possible amino acid residues, and examined their sensitivity to CM TRIM5a-mediated restriction. Results showed that hydrophobic residues or those with ring structures were associated with sensitivity, while those with small side chains or amide groups conferred resistance. Molecular dynamics simulation study revealed a structural basis for the differential TRIM5a sensitivities. The mutations at position 120 in the loop between helices 6 and 7 (L6/7) affected conformation of the neighboring loop between helices 4 and 5 (L4/5), and sensitive viruses had a common L4/5 conformation. In addition, the common L4/5 structures of the sensitive viruses were associated with a decreased probability of hydrogen bond
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