Tuyển tập các báo cáo nghiên cứu về sinh học được đăng trên tạp chí sinh học Journal of Biology đề tài: Decoding the multifaceted HIV-1 virus-host interactome. | Journal of Biology Minireview Decoding the multifaceted HIV-1 virus-host interactome Eric Y Chan Marcus J Korth and Michael G Katze Address Department of Microbiology University of Washington Seattle WA 98195-8070 USA. Correspondence Michael G Katze. Email honey@ Abstract Recently in BMC Medical Genomics Tozeren and colleagues have uncovered virus-host interactions by searching for conserved peptide motifs in HIV and human proteins. Their computational model provides a novel perspective in the interpretation of high-throughput data on the HIV-host interactome. The replication of the retrovirus HIV is no simple task. After binding to specific receptors on the cell surface fusion between the virion and the host membrane releases the viral core into the cytoplasm. The viral RNA genome is then reverse transcribed into DNA by the viral reverse transcriptase and the proviral DNA is integrated into the host genome. The host RNA polymerase II complex reads the integrated DNA and synthesizes viral RNA which is subsequently translated into proteins. All these viral products then have to be routed properly for assembly so that progeny virions can leave through the plasma membrane. As its genome encodes just 15 genes HIV depends on the coordinated actions of cellular factors throughout its replication cycle. However with more than 25 000 human protein-encoding genes to choose from according to RefSeq it is inconceivable that all of the approximately 1066 possible virus-host interaction combinations would be involved in virus replication. Computational prediction of protein interactions has typically been based on binding mediated by protein domains each of which can be up to 500 amino acids in size. However the limited size of the HIV gene products restricts the number of protein domains available for such analyses to put this in perspective the HIV Tat protein is composed of just 88 amino acids. In an alternative approach to the identification of virus-host .