Peptidylprolyl cis-trans isomerases of Legionella pneumophila: virulence, moonlighting and novel therapeutic targets

Yükleniyor...
Küçük Resim

Tarih

2014

Dergi Başlığı

Dergi ISSN

Cilt Başlığı

Yayıncı

Portland Press Ltd

Erişim Hakkı

info:eu-repo/semantics/closedAccess

Özet

Legionella pneumophila, typically a parasite of free-living protozoa, can also replicate in human alveolar macrophages and lung epithelial cells causing Legionnaires' disease in humans, a severe atypical pneumonia. The pathogen encodes six peptidylprolyl cis-trans isomerases (PPIases), which generally accelerate folding of prolyl peptide bonds, and influence protein folding. PPIases can be divided into three classes, cyclophilins, parvulins and FK506-binding proteins (FKBPs). They contribute to a multitude of cellular functions including bacterial virulence. In the present review, we provide an overview of L. pneumophila PPIases, discussing their known and anticipated functions as well as moonlighting phenomena. By taking the example of the macrophage infectivity potentiator (Mip) of L. pneumophila, we highlight the potential of PPIases as promising drug targets.

Açıklama

Unal, Can/0000-0003-4710-9567
WOS:000345427100041
PubMed: 25399597

Anahtar Kelimeler

Cyclophilin, Fk506-Binding Protein, Legionella Pneumophila, Moonlighting, Parvulin, Ppiase

Kaynak

Biochemical Society Transactions

WoS Q Değeri

Q2

Scopus Q Değeri

Q1

Cilt

42

Sayı

Künye