Characterization of N-Linked Protein Glycosylation in Helicobacter pullorum

Characterization of N-linked protein glycosylation in Helicobacter pullorum.

The first bacterial N-linked glycosylation system was discovered in Campylobacter jejuni, and the key enzyme involved in the coupling of glycan to asparagine residues within the acceptor sequon of the glycoprotein is the oligosaccharyltransferase PglB. Emerging genome sequence data have revealed that pglB orthologues are present in a subset of species from the Deltaproteobacteria and Epsilonpro...

Defective N-linked protein glycosylation pathway in congenital myasthenic syndromes.

Original Articles Rhythm-specific modulation of the sensorimotor network in drug-naı̈ve patients with Parkinson’s disease by levodopa F. Esposito, A. Tessitore, A. Giordano, R. De Micco, A. Paccone, R. Conforti, G. Pignataro, L. Annunziato and G. Tedeschi 710 Evidence for adaptive cortical changes in swallowing in Parkinson’s disease S. Suntrup, I. Teismann, J. Bejer, I. Suttrup, M. Winkels, D. ...

Helicobacter pullorum in Chickens, Belgium

A total of 110 broilers from 11 flocks were tested for Helicobacter pullorum by polymerase chain reaction; positive samples were reexamined with a conventional isolation method. H. pullorum isolates were examined by amplified fragment length polymorphism (AFLP) fingerprinting for interstrain genetic diversity and relatedness. Sixteen isolates from cecal samples from 2 different flocks were obta...

Mechanisms and principles of N-linked protein glycosylation.

N-linked glycosylation, a protein modification system present in all domains of life, is characterized by a high structural diversity of N-linked glycans found among different species and by a large number of proteins that are glycosylated. Based on structural, functional, and phylogenetic approaches, this review discusses the highly conserved processes that are at the basis of this unique gene...

Identification of an N-Linked Glycosylation