In silico analysis of ChtBD3 domain to find its role in bacterial pathogenesis and beyond

被引:6
作者
Patel, Seema [1 ]
Rauf, Abdur [2 ]
Meher, Biswa Ranjan [3 ]
机构
[1] San Diego State Univ, Bioinformat & Med Informat Res Ctr, 5500 Campanile Dr, San Diego, CA 92182 USA
[2] Univ Swabi, Dept Chem, Anbar 23561, Khyber Pakhtunk, Pakistan
[3] Cent Univ Jharkhand, Ctr Life Sci, Ranchi 835205, Bihar, India
关键词
Domain; ChtBD3; Pathogenesis; Glycosyl hydrolase; Chitinase; Peptidase; CHITIN-BINDING DOMAIN; BACILLUS-CIRCULANS WL-12; C-TERMINAL DOMAIN; MARINE BACTERIUM; VIBRIO-CHOLERAE; LISTERIA-MONOCYTOGENES; HYPOTHETICAL PROTEINS; EXTRACELLULAR PROTEIN; FUNCTIONAL-ANALYSIS; CATALYTIC DOMAIN;
D O I
10.1016/j.micpath.2017.07.047
中图分类号
R392 [医学免疫学]; Q939.91 [免疫学];
学科分类号
100102 ;
摘要
Chitin binding domain 3, known by the acronym ChtBD3, is a domain in the enzymes and proteins of several pathogenic virus, bacteria and fungi. As this domain is evolutionarily-conserved in virulence factors of these infectious agents, its detailed investigation is of clinical interest. In this regard, the current in silico study analyzed ChtBD3 domain distribution in bacterial proteins present in publicly available SMART (simple modular architecture research tool) database. Also, the co-occurring domains of ChtBD3 in the studied proteins were mapped to understand positional rearrangement of the domain and consequent functional diversity. Custom-made scripts were used to interpret the data and to derive patterns. As expected, interesting results were obtained. ChtBD3 domain co-occurred with other critical domains like peptidase, glycol_hydrolase, kinase, hemagglutinin-acting, collagen-binding, among others. The findings are expected to be of clinical relevance. (C) 2017 Elsevier Ltd. All rights reserved.
引用
收藏
页码:519 / 526
页数:8
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