NarE:: a novel ADP-ribosyltransferase from Neisseria meningitidis

被引:28
作者
Masignani, V
Balducci, E
Di Marcello, F
Savino, S
Serruto, D
Veggi, D
Bambini, S
Scarselli, M
Aricò, B
Comanducci, M
Adu-Bobie, J
Giuliani, MM
Rappuoli, R
Pizza, M
机构
[1] Chiron SRL, IRIS, I-53100 Siena, Italy
[2] Univ Camerino, Dipartimento Sci Morfol & Biochim Comparate, I-62032 Camerino, Italy
关键词
D O I
10.1046/j.1365-2958.2003.03770.x
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Mono ADP-ribosyltransferases (ADPRTs) are a class of functionally conserved enzymes present in prokaryotic and eukaryotic organisms. In bacteria, these enzymes often act as potent toxins and play an important role in pathogenesis. Here we report a profile-based computational approach that, assisted by secondary structure predictions, has allowed the identification of a previously undiscovered ADP-ribosyltransferase in Neisseria meningitidis (NarE). NarE shows structural homologies with E. coli heat-labile enterotoxin (LT) and cholera toxin (CT) and possesses ADP-ribosylating and NAD-glycohydrolase activities. As in the case of LT and CT, NarE catalyses the transfer of the ADP-ribose moiety to arginine residues. Despite the absence of a signal peptide, the protein is efficiently exported into the periplasm of Neisseria. The narE gene is present in 25 out of 43 strains analysed, is always present in ET-5 and Lineage 3 but absent in ET-37 and Cluster A4 hypervirulent lineages. When present, the gene is 100% conserved in sequence and is inserted upstream of and co-transcribed with the lipoamide dehydrogenase E3 gene. Possible roles in the pathogenesis of N. meningitidis are discussed.
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收藏
页码:1055 / 1067
页数:13
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