Premium
Analysis of post‐translational modification of mycobacterial proteins using a cassette expression system
Author(s) -
Herrmann Jean Louis,
Delahay Robin,
Gallagher Alex,
Robertson Brian,
Young Douglas
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01553-2
Subject(s) - glycosylation , glycoprotein , threonine , recombinant dna , n linked glycosylation , biochemistry , peptide sequence , biology , amino acid , chemistry , computational biology , gene , phosphorylation , serine , glycan
A recombinant expression system was developed to analyse sequence determinants involved in O ‐glycosylation of proteins in mycobacteria. By expressing peptide sequences corresponding to known glycosylation sites within a chimeric lipoprotein construct, amino acids flanking modified threonine residues were found to have an important influence on glycosylation. The expression system was used to screen mycobacterial sequences selected using a neural network (NetOglyc) trained on eukaryotic O ‐glycoproteins. Evidence of glycosylation was obtained for eight of 11 proteins tested. The results suggest that sites involved in O ‐glycosylation of mycobacterial and eukaryotic proteins share similar structural features.