Please use this identifier to cite or link to this item: https://hdl.handle.net/2440/28199
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Type: Journal article
Title: Virulence of Streptococcus pneumoniae: PsaA mutants are hypersensitive to oxidative stress
Author: Tseng, H.
McEwan, A.
Paton, J.
Jennings, M.
Citation: Infection and Immunity, 2002; 70(3):1635-1639
Publisher: Amer Soc Microbiology
Issue Date: 2002
ISSN: 0019-9567
1098-5522
Statement of
Responsibility: 
Hsing-Ju Tseng, Alastair G. McEwan, James C. Paton, and Michael P. Jennings
Abstract: psaA encodes a 37-kDa pneumococcal lipoprotein which is part of an ABC Mn(II) transport complex. Streptococcus pneumoniae D39 psaA mutants have previously been shown to be significantly less virulent than wild-type D39, but the mechanism underlying the attenuation has not been resolved. In this study, we have shown that psaA and psaD mutants are highly sensitive to oxidative stress, i.e., to superoxide and hydrogen peroxide, which might explain why they are less virulent than the wild-type strain. Our investigations revealed altered expression of the key oxidative-stress response enzymes superoxide dismutase and NADH oxidase in psaA and psaD mutants, suggesting that PsaA and PsaD may play important roles in the regulation of expression of oxidative-stress response enzymes and intracellular redox homeostasis.
Keywords: Streptococcus pneumoniae
Hydrogen Peroxide
Cations, Divalent
Manganese
Paraquat
Multienzyme Complexes
NADH, NADPH Oxidoreductases
Superoxide Dismutase
Lipoproteins
Bacterial Proteins
Adhesins, Bacterial
Carrier Proteins
Membrane Transport Proteins
Oxidative Stress
Mutation
Description: Copyright © 2002, American Society for Microbiology. All Rights Reserved.
DOI: 10.1128/IAI.70.3.1635-1639.2002
Description (link): http://iai.asm.org/content/vol70/issue10/index.dtl
Published version: http://dx.doi.org/10.1128/iai.70.3.1635-1639.2002
Appears in Collections:Aurora harvest 2
Molecular and Biomedical Science publications

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