Since PTMs are critical to PPIs, they should be taken into consideration when analyzing the effects
of different PPIs on host pathology. Meanwhile, PTM by itself is actually critical to host-virus interactions. Glycosylation, for example, is widely known to be critical to viral recognition and entrance into target cells. Given the wide spectrum of biological functions in which PTMs are involved, variations in host protein PTM patterns should have major impacts on immune response and virus life cycle. Thirdly, one surprising finding here is that PTMs actually differ to a great extent among the four compared species, considering that they are genetically close to one another. For example, human and chimpanzee differ from each other by Cell Cycle inhibitor an average of two amino acids per protein [11]. In comparison, in the 1,370 proteins compared, human and chimpanzee each has more than 600 species-specific substitution-related phosphorylation sites (Table 3). In other words, on average, each HIV-interacting protein in both human and chimpanzee has an average of 0.4 species-specific phosphorlation sites. This example illustrates the importance of “”PTMome”". Glycome, the collective sum of all glycans and part of the PTMome (if glycolipids are not considered), is known to be
remarkably larger than proteome [43, 44]. Therefore, it is easily understandable that Torin 1 manufacturer PTMome is actually much larger than proteome. The large numbers of species-specific PTMs in HIV-interacting proteins illustrate the great potential of PTM studies in virology and AIDS studies. Conclusion The CAPIH interface is unique because it is the first web-based tool to provide comparative information of genetic changes and PTMs in host-pathogen interactions. Since cross-species fantofarone viral infections have become a critical issue in public health, comparative studies of host-pathogen interactions deserve wide attention. Specifically, comparative analyses of host-HIV interactions may shed some light on the mechanisms of differences in AIDS progression between human and chimpanzee. A number of possible mechanisms have been proposed [8, 45]. However, none of them provides a systematic view in the context
of host-HIV protein interactions. Furthermore, PTMs, perhaps one of the most important regulatory mechanisms of host-pathogen protein interactions, have been rarely studied in a comparative way. This interface may provide clues to the potential roles of PTMs in HIV infections, and serve as a starting point for studies on host-HIV protein interaction networks in different hosts. Availability and requirements The CAPIH database is available at http://bioinfo-dbb.nhri.org.tw/hivppi/. The JAVA Runtime Environment is required to view the interactive protein networks. Acknowledgements FCC is supported by by National Health Research Institutes (NHRI) check details intramural funding and the National Science Council, Taiwan (under contract NSC 97-3112-B-400-015 and NSC 98-2311-B-400-002-MY3).