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Cloning and characterization of a novel PE_PGRS60 protein (Rv3652) of Mycobacterium tuberculosis H 37 Rv exhibit fibronectin‐binding property
Author(s) -
Meena Laxman S.,
Meena Jaishree
Publication year - 2015
Publication title -
biotechnology and applied biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 70
eISSN - 1470-8744
pISSN - 0885-4513
DOI - 10.1002/bab.1411
Subject(s) - fibronectin , mycobacterium tuberculosis , epitope , biology , cloning (programming) , peptide sequence , cleavage (geology) , microbiology and biotechnology , mycobacterium , biochemistry , extracellular matrix , antigen , tuberculosis , bacteria , gene , genetics , paleontology , pathology , fracture (geology) , computer science , programming language , medicine
The binding of pathogenic bacteria to extracellular matrix components enhances adhesion and invasion of host cells. The host receptor proteins such as fibronectin (Fn) targeted to pathogenic ligands that have clinical importance. In the present study, we cloned, expressed, purified, and identified a novel Fn‐binding protein from PE_PGRS60 (Rv3652) of Mycobacterium tuberculosis H 37 Rv. The protein product of Rv3652 showed optimum binding efficiency to 10 ng Fn at 0.2 µg purified protein of PE_PGRS60 and 20 ng Fn at 0.2 µg concentrations, respectively. PE_PGRS60 protein (primary sequences) of different pathogenic mycobacterium species retrieved from NCBI exhibited complete homology at the 104 residues on multiple sequence alignment. The primary sequence of protein from H 37 Rv was further used to predict cleavage signals. The secondary structure prediction method revealed a number of residues responsible for alpha helices formation and percentage of residues participating in the random coils and extended strands. In addition, online prediction tools such as B‐ and T‐cell epitopes showed the surface probability scale and antigenic propensity scale. The current finding opens new opportunity to mycobacterial survival and pathogenesis research of PE‐polymorphic GC‐rich repetitive sequences (PE‐PGRS) family proteins.