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Background  To date, the function of many hypothetical membrane proteins of  Mycobacterium tuberculosis  is still unknown and their involvement in pathogen-host interactions has not been yet clearly defined. In this study, the biological activity of peptides derived from the hypothetical membrane protein Rv0679c of  M. tuberculosis  and their involvement in pathogen-host interactions was assessed. Transcription of the  Rv0679c  gene was studied in 26  Mycobacterium  spp. Strains. Antibodies raised against putative B-cell epitopes of Rv0679c were used in Western blot and immunoelectron microscopy assays. Synthetic peptides spanning the entire length of the protein were tested for their ability to bind to A549 and U937 cells. High-activity binding peptides (HABPs) identified in Rv0679c were tested for their ability to inhibit mycobacterial invasion into cells.    Results  The gene encoding Rv0679c was detected in all strains of the  M. tuberculosis  complex (MTC), but was only transcribed in  M. tuberculosis  H37Rv,  M. tuberculosis  H37Ra and  M. africanum . Anti-Rv0679c antibodies specifically recognized the protein in  M. tuberculosis  H37Rv sonicate and showed its localization on mycobacterial surface. Four HABPs inhibited invasion of  M. tuberculosis  to target cells by up to 75%.    Conclusions  The results indicate that Rv0679c HABPs and in particular HABP 30979 could be playing an important role during  M. tuberculosis  invasion of host cells, and therefore could be interesting research targets for studies aimed at developing strategies to control tuberculosis.

Mycobacterium tuberculosis Rv0679c protein sequences involved in host-cell infection: Potential TB vaccine candidate antigen