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Roles of the Peptide Transport Systems and Aminopeptidase PepA in Peptide Assimilation by Helicobacter pylori

Authors
Ki, Mi RanLee, Ji HyunYun, Soon KyuChoi, Kyung MinHwang, Se Young
Issue Date
10월-2015
Publisher
KOREAN SOC MICROBIOLOGY & BIOTECHNOLOGY
Keywords
Helicobacter pylori; peptide transport; PepTs; PepA; detector peptides
Citation
JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY, v.25, no.10, pp.1629 - 1633
Indexed
SCIE
SCOPUS
KCI
Journal Title
JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY
Volume
25
Number
10
Start Page
1629
End Page
1633
URI
https://scholar.korea.ac.kr/handle/2021.sw.korea/92341
DOI
10.4014/jmb.1505.05099
ISSN
1017-7825
Abstract
Peptide assimilation in Helicobacter pylori necessitates a coordinated working of the peptide transport systems (PepTs) and aminopeptidase (PepA). We found that H. pylori hydrolyzes two detector peptides, L-phenylalanyl-L-3-thiaphenylalanine (PSP) and L-phenylalanyl-L-2-sulfanilylglycine (PSG), primarily before intake and excludes their antibacterial effects, whereas Escherichia coli readily transports them with resultant growth inhibition. PSP assimilation by H. pylori was inhibited by aminopeptidase inhibitor bestatin, but not by dialanine or cyanide-m-chlorophenylhydrazone, contrary to that of E. coli. RT- and qRT-PCR analyses showed that H. pylori may express first the PepTs (e.g., DppA and DppB) and then PepA. In addition, western blot analysis of PepA suggested that the bacterium secretes PepA in response to specific inducers.
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