Abstract
PE/PPE family proteins, named after their conserved PE (Pro-Glu) and PPE (Pro-Pro-Glu) domains of N-terminal, are most intriguing aspects of pathologic mycobacterial genome. The roles of most members of this family remain unknown, although selected genes of this family are related to the virulence of Mycobacterium tuberculosis. In order to decipher the role of Rv1169c, the Mycobacterium smegmatis strain heterologous expressed this ORF was constructed and identified that Rv1169c was a cell wall associated protein with a novel function in modifying the cell wall fatty acids. The growth of Rv1169c expressing strain was affected under surface stress, acidic condition and antibiotics treatment. M. smegmatis expressing Rv1169c induced necrotic cell death of macrophage after infection and significantly decreased interlukin-6 production compared to controls. In general, these results underscore a proposing role of Rv1169c in virulence of M. tuberculosis, as it's role in the susceptibility of anti-mycobacteria factors caused by modified cell wall fatty acid, and the induced necrotic cell death by Rv1169c is crucial for M. tuberculosis virulence during infection.
Highlights
Tuberculosis (TB), caused by Mycobacterium tuberculosis infection, remains a formidable threat to global public health
Our studies demonstrated that M. smegmatis expressing Rv1169c has a modified cell wall fatty acid consonant, and its ability to against anti-tuberculosis factors was abated
M. tuberculosis Rv1169c Can Be Expressed in M. smegmatis M. tuberculosis PE/PPE family Rv1169c gene encodes 12 kDa protein with about 300 bp in size
Summary
Tuberculosis (TB), caused by Mycobacterium tuberculosis infection, remains a formidable threat to global public health. The function of M. tuberculosis Rv1169c motif (Cole and Barrell, 1998; Cole et al, 1998) and about 100 genes encoding PE subfamily, which harbor a conserved N-terminal domain with 110 amino acid residues with the Pro-Glu (PE) motif, while the C-termini vary significantly in size and protein-specific polymorphic GC-rich repeats PGRS (Cole et al, 1998; Akhter et al, 2012). The 69 PPE proteins are classified into PPE_SVP with typical G-X-S-V-P-X-X-W repeats, PPE_PPW with special G-F-X-G-T and Pro-X-X-P-XX-W sequences and PPE_MPTR with N-X-G-X-G-N-A-G major polymorphic tandem motifs in their C terminal (Cole and Barrell, 1998; Cole et al, 1998). The unique sequences of these proteins might underlie the specific physiological role of this family during M. tuberculosis infection
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