Oligopeptidase B, a missing enzyme in mammals and a potential drug target for trypanosomatid diseases.
Animals
Chagas Disease
/ parasitology
Humans
Leishmania
/ enzymology
Leishmaniasis
/ parasitology
Mammals
Protozoan Proteins
/ chemistry
Serine Endopeptidases
/ chemistry
Trypanosoma brucei brucei
/ enzymology
Trypanosoma cruzi
/ enzymology
Trypanosomiasis, African
/ parasitology
Virulence Factors
/ chemistry
Drug target
Leishmania
Oligopeptidase B
Serine protease
Trypanosoma brucei
Trypanosoma cruzi
Journal
Biochimie
ISSN: 1638-6183
Titre abrégé: Biochimie
Pays: France
ID NLM: 1264604
Informations de publication
Date de publication:
Dec 2019
Dec 2019
Historique:
received:
24
07
2019
accepted:
15
10
2019
pubmed:
20
10
2019
medline:
7
1
2020
entrez:
20
10
2019
Statut:
ppublish
Résumé
Oligopeptidases B (OPB) belong to the S9 prolyl oligopeptidase family and are expressed in prokaryotes, some eukaryotes and in some higher plants. OPB is not found in any of the mammalian genomes available to date. Evidences indicate that OPB participates in the infections caused by trypanosomatids Trypanosoma cruzi, Leishmania spp. and Trypanosoma brucei spp and therefore it is considered an important virulence factor. Trypanosomatids from the genera Leishmania and Trypanosoma also present other OPB, named OPB2. A more accurate investigation of trypanosomatid OPB sequences brought attention to what could be a third OPB sequence (OPB3). This review aims to discuss biochemical, structural, phylogenetic and functional properties of OPB and its potential as target for the development of drugs against Chagas disease, leishmaniasis and African trypanosomiasis.
Identifiants
pubmed: 31628976
pii: S0300-9084(19)30299-8
doi: 10.1016/j.biochi.2019.10.006
pii:
doi:
Substances chimiques
Protozoan Proteins
0
Virulence Factors
0
Serine Endopeptidases
EC 3.4.21.-
oligopeptidase B
EC 3.4.21.83
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
207-216Informations de copyright
Copyright © 2019 Elsevier B.V. and Société Française de Biochimie et Biologie Moléculaire (SFBBM). All rights reserved.