Oligosaccharyltransferase PglB of Campylobacter jejuni is a glycoprotein.

Szczegóły
Abstrakt

Tytuł:: Oligosaccharyltransferase PglB of Campylobacter jejuni is a glycoprotein.
Autorzy:: Bokhari H; Department of Biosciences, COMSATS University, Islamabad, Chak Shazad Campus, Islamabad, Pakistan. .
Maryam A; Department of Biosciences, COMSATS University, Islamabad, Chak Shazad Campus, Islamabad, Pakistan.
Shahid R; Department of Biosciences, COMSATS University, Islamabad, Chak Shazad Campus, Islamabad, Pakistan.
Siddiqi AR; Department of Biosciences, COMSATS University, Islamabad, Chak Shazad Campus, Islamabad, Pakistan.
Źródło:: World journal of microbiology & biotechnology [World J Microbiol Biotechnol] 2019 Dec 19; Vol. 36 (1), pp. 9. Date of Electronic Publication: 2019 Dec 19.
Typ publikacji:: Journal Article
Język:: English
Imprint Name(s):: Publication: 2005- : Berlin : Springer
Original Publication: Oxford, OX, UK : Published by Rapid Communications of Oxford Ltd in association with UNESCO and in collaboration with the International Union of Microbiological Societies, c1990-
MeSH Terms:: Campylobacter jejuni/*enzymology
Glycoproteins/*chemistry
Hexosyltransferases/*chemistry
Membrane Proteins/*chemistry
Amino Acid Sequence ; Bacterial Outer Membrane Proteins/genetics ; Bacterial Proteins/genetics ; Glycosylation ; Hexosyltransferases/genetics ; Hexosyltransferases/immunology ; Membrane Proteins/genetics ; Membrane Proteins/immunology ; Models, Molecular ; Mutagenesis, Site-Directed ; Phylogeny ; Protein Conformation ; Sequence Alignment ; Sequence Analysis, Protein ; Vaccines
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Grant Information:: NRPU Higher Education Commision, Pakistan
Contributed Indexing:: Keywords: C. jejuni; Glycoproteins; Glycosylation; Oligosaccharyltransferase; PglB; Vaccine
Substance Nomenclature:: 0 (Bacterial Outer Membrane Proteins)
0 (Bacterial Proteins)
0 (Glycoproteins)
0 (Membrane Proteins)
0 (Vaccines)
134944-14-2 (ompH protein, bacteria)
EC 2.4.1.- (Hexosyltransferases)
EC 2.4.99.18 (dolichyl-diphosphooligosaccharide - protein glycotransferase)
Entry Date(s):: Date Created: 20191221 Date Completed: 20200121 Latest Revision: 20200122
Update Code:: 20240105
DOI:: 10.1007/s11274-019-2784-9
PMID:: 31858269
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Campylobacter jejuni is the one of the leading cause of bacterial food borne gastroenteritis. PglB, a glycosyltransferase, plays a crucial role of mediating glycosylation of numerous periplasmic proteins. It catalyzes N-glycosylation at the sequon D/E-X1-N-X2-S/T in its substrate proteins. Here we report that the PglB itself is a glycoprotein which self-glycosylates at N534 site in its DYNQS sequon by its own catalytic WWDYG motif. Site-directed mutagenesis, lectin Immunoblot, and mobility shift assays confirmed that the DYNQS is an N-glycosylation motif. PglB's N-glycosylation motif is structurally and functionally similar to its widely studied glycosylation substrate, the OMPH1. Its DYNQS motif forms a solvent-exposed crest. This motif is close to a cluster of polar and hydrophilic residues, which form a loop flanked by two α helices. This arrangement extremely apposite for auto-glycosylation at N534. This self-glycosylation ability of PglB could mediate C. jejuni's ability to colonize the intestinal epithelium. Further this capability may also bear significance for the development of novel conjugated vaccines and diagnostic tests.

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