Abstract:
:Bacterial ADP-ribosyltransferases (BADPRTs) are extensively contributed to determine the strain-specific virulence state and pathogenesis in human hosts. Understanding molecular evolution and functional diversity of the BADPRTs is an important standpoint to describe the fundamental behind in the vaccine designing for bacterial infections. In the present study, we have evaluated the origin and functional evolution of conserved domains within the BADPRTs by analyzing their sequence-function relationship. To represent the evolution history of BADPRTs, phylogenetic trees were constructed based on their protein sequence, structure and conserved domains using different evolutionary programs. Sequence divergence and genetic diversity were studied herein to deduce the functional evolution of conserved domains across the family and superfamily. The results of sequence similarity search have shown that three hypothetical proteins (above 90%) were identical to the members of BADPRTs and their functions were annotated by phylogenetic approach. Phylogenetic analysis of this study has revealed the family members of BADPRTs were phylogenetically related to one another, functionally diverged within the same family, and dispersed into closely related bacteria. The presence of core substitution pattern in the conserved domains would determine the family-specific function of BADPRTs. Functional diversity of the BADPRTs was exclusively distinguished by Darwinian positive selection (diphtheria toxin C and pertussis toxin S) and neutral selection (arginine ADP-ribosyltransferase, enterotoxin A and binary toxin A) acting on the existing domains. Many of the family members were sharing their sequence-specific features from members in the arginine ADP-ribosyltransferase family. Conservative functions of members in the BADPRTs have shown to be expanded only within closely related families, and retained as such in pathogenic bacteria by evolutionary process (domain duplication or recombination events). Hence, we conclude that evolutionary significance of the members in the BADPRTs would provide an insight for experimental set-up on site-directed mutagenesis and vaccine engineering.
journal_name
Protein Pept Lettjournal_title
Protein and peptide lettersauthors
Chellapandi P,Sakthishree S,Bharathi Mdoi
10.2174/0929866511320090012subject
Has Abstractpub_date
2013-09-01 00:00:00pages
1054-65issue
9eissn
0929-8665issn
1875-5305pii
PPL-EPUB-20130409-1journal_volume
20pub_type
杂志文章abstract:BACKGROUND:A core sequence (the 9 C-terminal residues) of calcification-associated peptide (CAP- 1) isolated from the exoskeleton of the red swamp crayfish was previously shown to control calcium carbonate precipitation with chitin. In addition, a modified core sequence in which the phosphorylated serine at the N termi...
journal_title:Protein and peptide letters
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journal_title:Protein and peptide letters
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journal_title:Protein and peptide letters
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journal_title:Protein and peptide letters
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journal_title:Protein and peptide letters
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journal_title:Protein and peptide letters
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journal_title:Protein and peptide letters
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journal_title:Protein and peptide letters
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journal_title:Protein and peptide letters
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journal_title:Protein and peptide letters
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journal_title:Protein and peptide letters
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journal_title:Protein and peptide letters
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更新日期:2003-12-01 00:00:00
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journal_title:Protein and peptide letters
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journal_title:Protein and peptide letters
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journal_title:Protein and peptide letters
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journal_title:Protein and peptide letters
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journal_title:Protein and peptide letters
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journal_title:Protein and peptide letters
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journal_title:Protein and peptide letters
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