<HashMap><database>biostudies-literature</database><scores><citationCount>0</citationCount><reanalysisCount>0</reanalysisCount><viewCount>46</viewCount><searchCount>0</searchCount></scores><additional><submitter>Hoopman TC</submitter><funding>NIAID NIH HHS</funding><pagination>745-55</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC3028835</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>79(2)</volume><pubmed_abstract>Moraxella catarrhalis is subjected to oxidative stress from both internal and environmental sources. A previous study (C. D. Pericone, K. Overweg, P. W. Hermans, and J. N. Weiser, Infect. Immun. 68:3990-3997, 2000) indicated that a wild-type strain of M. catarrhalis was very resistant to killing by exogenous hydrogen peroxide (H₂O₂). The gene encoding OxyR, a LysR family transcriptional regulator, was identified and inactivated in M. catarrhalis strain O35E, resulting in an increase in sensitivity to killing by H₂O₂ in disk diffusion assays and a concomitant aerobic serial dilution effect. Genes encoding a predicted catalase (KatA) and an alkyl hydroperoxidase (AhpCF) showed dose-dependent upregulation in wild-type cells exposed to H₂O₂. DNA microarray and real-time reverse transcription-PCR (RT-PCR) analyses identified M. catarrhalis genes whose expression was affected by oxidative stress in an OxyR-dependent manner. Testing of M. catarrhalis O35E katA and ahpC mutants for their abilities to scavenge exogenous H₂O₂ showed that the KatA catalase was responsible for most of this activity in the wild-type parent strain. The introduction of the same mutations into M. catarrhalis strain ETSU-4 showed that the growth of a ETSU-4 katA mutant was markedly inhibited by the addition of 50 mM H₂O₂ but that this mutant could still form a biofilm equivalent to that produced by its wild-type parent strain.</pubmed_abstract><journal>Infection and immunity</journal><pubmed_title>Identification of gene products involved in the oxidative stress response of Moraxella catarrhalis.</pubmed_title><pmcid>PMC3028835</pmcid><funding_grant_id>5-T32-AI007520</funding_grant_id><funding_grant_id>AI36344</funding_grant_id><funding_grant_id>AI076365</funding_grant_id><funding_grant_id>T32 AI007520</funding_grant_id><funding_grant_id>R01 AI036344</funding_grant_id><funding_grant_id>K08 AI076365</funding_grant_id><pubmed_authors>Pybus C</pubmed_authors><pubmed_authors>Hansen EJ</pubmed_authors><pubmed_authors>Hoopman TC</pubmed_authors><pubmed_authors>Joslin SN</pubmed_authors><pubmed_authors>Brautigam CA</pubmed_authors><pubmed_authors>Liu W</pubmed_authors><view_count>46</view_count></additional><is_claimable>false</is_claimable><name>Identification of gene products involved in the oxidative stress response of Moraxella catarrhalis.</name><description>Moraxella catarrhalis is subjected to oxidative stress from both internal and environmental sources. A previous study (C. D. Pericone, K. Overweg, P. W. Hermans, and J. N. Weiser, Infect. Immun. 68:3990-3997, 2000) indicated that a wild-type strain of M. catarrhalis was very resistant to killing by exogenous hydrogen peroxide (H₂O₂). The gene encoding OxyR, a LysR family transcriptional regulator, was identified and inactivated in M. catarrhalis strain O35E, resulting in an increase in sensitivity to killing by H₂O₂ in disk diffusion assays and a concomitant aerobic serial dilution effect. Genes encoding a predicted catalase (KatA) and an alkyl hydroperoxidase (AhpCF) showed dose-dependent upregulation in wild-type cells exposed to H₂O₂. DNA microarray and real-time reverse transcription-PCR (RT-PCR) analyses identified M. catarrhalis genes whose expression was affected by oxidative stress in an OxyR-dependent manner. Testing of M. catarrhalis O35E katA and ahpC mutants for their abilities to scavenge exogenous H₂O₂ showed that the KatA catalase was responsible for most of this activity in the wild-type parent strain. The introduction of the same mutations into M. catarrhalis strain ETSU-4 showed that the growth of a ETSU-4 katA mutant was markedly inhibited by the addition of 50 mM H₂O₂ but that this mutant could still form a biofilm equivalent to that produced by its wild-type parent strain.</description><dates><release>2011-01-01T00:00:00Z</release><publication>2011 Feb</publication><modification>2024-12-04T08:04:20.891Z</modification><creation>2019-03-27T00:38:27Z</creation></dates><accession>S-EPMC3028835</accession><cross_references><pubmed>21098105</pubmed><doi>10.1128/iai.01060-10</doi><doi>10.1128/IAI.01060-10</doi></cross_references></HashMap>