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Thioredoxin A of Streptococcus suis Serotype 2 Contributes to Virulence by Inhibiting the Expression of Pentraxin 3 to Promote Survival Within Macrophages
Streptococcus suis serotype 2 (SS2) is an important zoonotic pathogen that can infect humans in contact with infected pigs or their byproducts. It can employ different types of genes to defend against oxidative stress and ensure its survival. The thioredoxin (Trx) system is a key antioxidant system...
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Published in: | The journal of microbiology 2023-04, Vol.61 (4), p.433-448 |
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creator | Zhao, Chijun Jia, Xinglin Pan, Yanying Liao, Simeng Zhang, Shuo Ji, Chunxiao Kuang, Guangwei Wu, Xin Liu, Quan Tang, Yulong Fang, Lihua |
description | Streptococcus suis
serotype 2 (SS2) is an important zoonotic pathogen that can infect humans in contact with infected pigs or their byproducts. It can employ different types of genes to defend against oxidative stress and ensure its survival. The thioredoxin (Trx) system is a key antioxidant system that contributes adversity adaptation and pathogenicity. SS2 has been shown to encode putative thioredoxin genes, but the biological roles, coding sequence, and underlying mechanisms remains uncharacterized. Here, we demonstrated that SSU05_0237-ORF, from a clinical SS2 strain, ZJ081101, encodes a protein of 104 amino acids with a canonical CGPC active motif and an identity 70–85% similar to the thioredoxin A (TrxA) in other microorganisms. Recombinant TrxA efficiently catalyzed the thiol-disulfide oxidoreduction of insulin. The deletion of TrxA led to a significantly slow growth and markedly compromised tolerance of the pathogen to temperature stress, as well as impaired adhesion ability to pig intestinal epithelial cells (IPEC-J2). However, it was not involved in H
2
O
2
and paraquat-induced oxidative stress. Compared with the wild-type strain, the ΔTrxA strain was more susceptible to killing by macrophages through increasing NO production. Treatment with TrxA mutant strain also significantly attenuated cytotoxic effects on RAW 264.7 cells by inhibiting inflammatory response and apoptosis. Knockdown of pentraxin 3 in RAW 264.7 cells was more vulnerable to phagocytic activity, and TrxA promoted SS2 survival in phagocytic cells depending on pentraxin 3 activity compared with the wild-type strain. Moreover, a co-inoculation experiment in mice revealed that TrxA mutant strain is far more easily cleared from the body than the wild type strain in the period from 8–24 h, and exhibits significantly attenuated oxidative stress and liver injury. In summary, we reveal the important role of TrxA in the pathogenesis of SS2. |
doi_str_mv | 10.1007/s12275-023-00038-4 |
format | article |
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serotype 2 (SS2) is an important zoonotic pathogen that can infect humans in contact with infected pigs or their byproducts. It can employ different types of genes to defend against oxidative stress and ensure its survival. The thioredoxin (Trx) system is a key antioxidant system that contributes adversity adaptation and pathogenicity. SS2 has been shown to encode putative thioredoxin genes, but the biological roles, coding sequence, and underlying mechanisms remains uncharacterized. Here, we demonstrated that SSU05_0237-ORF, from a clinical SS2 strain, ZJ081101, encodes a protein of 104 amino acids with a canonical CGPC active motif and an identity 70–85% similar to the thioredoxin A (TrxA) in other microorganisms. Recombinant TrxA efficiently catalyzed the thiol-disulfide oxidoreduction of insulin. The deletion of TrxA led to a significantly slow growth and markedly compromised tolerance of the pathogen to temperature stress, as well as impaired adhesion ability to pig intestinal epithelial cells (IPEC-J2). However, it was not involved in H
2
O
2
and paraquat-induced oxidative stress. Compared with the wild-type strain, the ΔTrxA strain was more susceptible to killing by macrophages through increasing NO production. Treatment with TrxA mutant strain also significantly attenuated cytotoxic effects on RAW 264.7 cells by inhibiting inflammatory response and apoptosis. Knockdown of pentraxin 3 in RAW 264.7 cells was more vulnerable to phagocytic activity, and TrxA promoted SS2 survival in phagocytic cells depending on pentraxin 3 activity compared with the wild-type strain. Moreover, a co-inoculation experiment in mice revealed that TrxA mutant strain is far more easily cleared from the body than the wild type strain in the period from 8–24 h, and exhibits significantly attenuated oxidative stress and liver injury. In summary, we reveal the important role of TrxA in the pathogenesis of SS2.</description><identifier>ISSN: 1225-8873</identifier><identifier>EISSN: 1976-3794</identifier><identifier>DOI: 10.1007/s12275-023-00038-4</identifier><identifier>PMID: 37010796</identifier><language>eng</language><publisher>Seoul: The Microbiological Society of Korea</publisher><subject>adhesion ; Amino acids ; Animals ; antioxidants ; Apoptosis ; Bacteria ; Bacterial Proteins - metabolism ; Biomedical and Life Sciences ; Cytotoxicity ; Epithelial cells ; Epithelium ; Genes ; Humans ; Hydrogen peroxide ; Hydrogen Peroxide - metabolism ; Hydrogen Peroxide - pharmacology ; Inflammation ; Inflammatory response ; Inoculation ; Insulin ; intestines ; Life Sciences ; liver ; Macrophages ; Macrophages - metabolism ; Mice ; Microbial Pathogenesis and Host-Microbe Interaction ; Microbiology ; Microorganisms ; Mutants ; Open reading frames ; Oxidative stress ; Oxidoreductions ; Paraquat ; Pathogenesis ; Pathogenicity ; Pathogens ; Pentraxins ; Phagocytes ; phagocytosis ; Recombinants ; Serogroup ; serotypes ; Streptococcal Infections ; Streptococcus infections ; Streptococcus suis ; Streptococcus suis - metabolism ; Survival ; Swine ; temperature ; Temperature tolerance ; Thioredoxin ; thioredoxins ; Thioredoxins - genetics ; Thioredoxins - metabolism ; Thioredoxins - pharmacology ; Virulence ; Virulence - genetics</subject><ispartof>The journal of microbiology, 2023-04, Vol.61 (4), p.433-448</ispartof><rights>The Author(s), under exclusive licence to Microbiological Society of Korea 2023. Springer Nature or its licensor (e.g. a society or other partner) holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law.</rights><rights>2023. The Author(s), under exclusive licence to Microbiological Society of Korea.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c408t-9b1d3a14356f7cc24fa27016e771581c8cbe6ec0dca12c7bf018d9fc22f450303</citedby><cites>FETCH-LOGICAL-c408t-9b1d3a14356f7cc24fa27016e771581c8cbe6ec0dca12c7bf018d9fc22f450303</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/37010796$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Zhao, Chijun</creatorcontrib><creatorcontrib>Jia, Xinglin</creatorcontrib><creatorcontrib>Pan, Yanying</creatorcontrib><creatorcontrib>Liao, Simeng</creatorcontrib><creatorcontrib>Zhang, Shuo</creatorcontrib><creatorcontrib>Ji, Chunxiao</creatorcontrib><creatorcontrib>Kuang, Guangwei</creatorcontrib><creatorcontrib>Wu, Xin</creatorcontrib><creatorcontrib>Liu, Quan</creatorcontrib><creatorcontrib>Tang, Yulong</creatorcontrib><creatorcontrib>Fang, Lihua</creatorcontrib><title>Thioredoxin A of Streptococcus suis Serotype 2 Contributes to Virulence by Inhibiting the Expression of Pentraxin 3 to Promote Survival Within Macrophages</title><title>The journal of microbiology</title><addtitle>J Microbiol</addtitle><addtitle>J Microbiol</addtitle><description>Streptococcus suis
serotype 2 (SS2) is an important zoonotic pathogen that can infect humans in contact with infected pigs or their byproducts. It can employ different types of genes to defend against oxidative stress and ensure its survival. The thioredoxin (Trx) system is a key antioxidant system that contributes adversity adaptation and pathogenicity. SS2 has been shown to encode putative thioredoxin genes, but the biological roles, coding sequence, and underlying mechanisms remains uncharacterized. Here, we demonstrated that SSU05_0237-ORF, from a clinical SS2 strain, ZJ081101, encodes a protein of 104 amino acids with a canonical CGPC active motif and an identity 70–85% similar to the thioredoxin A (TrxA) in other microorganisms. Recombinant TrxA efficiently catalyzed the thiol-disulfide oxidoreduction of insulin. The deletion of TrxA led to a significantly slow growth and markedly compromised tolerance of the pathogen to temperature stress, as well as impaired adhesion ability to pig intestinal epithelial cells (IPEC-J2). However, it was not involved in H
2
O
2
and paraquat-induced oxidative stress. Compared with the wild-type strain, the ΔTrxA strain was more susceptible to killing by macrophages through increasing NO production. Treatment with TrxA mutant strain also significantly attenuated cytotoxic effects on RAW 264.7 cells by inhibiting inflammatory response and apoptosis. Knockdown of pentraxin 3 in RAW 264.7 cells was more vulnerable to phagocytic activity, and TrxA promoted SS2 survival in phagocytic cells depending on pentraxin 3 activity compared with the wild-type strain. Moreover, a co-inoculation experiment in mice revealed that TrxA mutant strain is far more easily cleared from the body than the wild type strain in the period from 8–24 h, and exhibits significantly attenuated oxidative stress and liver injury. In summary, we reveal the important role of TrxA in the pathogenesis of SS2.</description><subject>adhesion</subject><subject>Amino acids</subject><subject>Animals</subject><subject>antioxidants</subject><subject>Apoptosis</subject><subject>Bacteria</subject><subject>Bacterial Proteins - metabolism</subject><subject>Biomedical and Life Sciences</subject><subject>Cytotoxicity</subject><subject>Epithelial cells</subject><subject>Epithelium</subject><subject>Genes</subject><subject>Humans</subject><subject>Hydrogen peroxide</subject><subject>Hydrogen Peroxide - metabolism</subject><subject>Hydrogen Peroxide - pharmacology</subject><subject>Inflammation</subject><subject>Inflammatory response</subject><subject>Inoculation</subject><subject>Insulin</subject><subject>intestines</subject><subject>Life Sciences</subject><subject>liver</subject><subject>Macrophages</subject><subject>Macrophages - metabolism</subject><subject>Mice</subject><subject>Microbial Pathogenesis and Host-Microbe Interaction</subject><subject>Microbiology</subject><subject>Microorganisms</subject><subject>Mutants</subject><subject>Open reading frames</subject><subject>Oxidative stress</subject><subject>Oxidoreductions</subject><subject>Paraquat</subject><subject>Pathogenesis</subject><subject>Pathogenicity</subject><subject>Pathogens</subject><subject>Pentraxins</subject><subject>Phagocytes</subject><subject>phagocytosis</subject><subject>Recombinants</subject><subject>Serogroup</subject><subject>serotypes</subject><subject>Streptococcal Infections</subject><subject>Streptococcus infections</subject><subject>Streptococcus suis</subject><subject>Streptococcus suis - metabolism</subject><subject>Survival</subject><subject>Swine</subject><subject>temperature</subject><subject>Temperature tolerance</subject><subject>Thioredoxin</subject><subject>thioredoxins</subject><subject>Thioredoxins - genetics</subject><subject>Thioredoxins - metabolism</subject><subject>Thioredoxins - pharmacology</subject><subject>Virulence</subject><subject>Virulence - genetics</subject><issn>1225-8873</issn><issn>1976-3794</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2023</creationdate><recordtype>article</recordtype><recordid>eNqFkc1u1DAUhSMEoj_wAiyQJTZsQu1rJ06W1aillYpaaQosLce5mbjKxMF2qs6r9GnrMAUkFrCypfudc3XuybJ3jH5ilMqTwABkkVPgOaWUV7l4kR2yWpY5l7V4mf4ARV5Vkh9kRyHcUVoyLuB1dsAlZVTW5WH2eNtb57F1D3Ykp8R1ZB09TtEZZ8wcSJhtIGv0Lu4mJEBWbozeNnPEQKIj36yfBxwNkmZHLsfeNjbacUNij-TsYfIYgnXjYnuDSaiXLXwR3ni3dRHJevb39l4P5LuNfRp-0ca7qdcbDG-yV50eAr59fo-zr-dnt6uL_Or68-Xq9Co3glYxrxvWcs0EL8pOGgOi05DilSglKypmKtNgiYa2RjMwsukoq9q6MwCdKCin_Dj7uPedvPsxY4hqa4PBYdAjujkozgrOasF4_V8U0t3LGmQJCf3wF3rnZj-mIAoqxqAQHBZD2FMpdQgeOzV5u9V-pxhVS8lqX7JKJaufJSuRRO-fredmi-1vya9WE8D3QEijcYP-z-5_2D4BnxSzgw</recordid><startdate>20230401</startdate><enddate>20230401</enddate><creator>Zhao, Chijun</creator><creator>Jia, Xinglin</creator><creator>Pan, Yanying</creator><creator>Liao, Simeng</creator><creator>Zhang, Shuo</creator><creator>Ji, Chunxiao</creator><creator>Kuang, Guangwei</creator><creator>Wu, Xin</creator><creator>Liu, Quan</creator><creator>Tang, Yulong</creator><creator>Fang, Lihua</creator><general>The Microbiological Society of Korea</general><general>Springer Nature B.V</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>7T7</scope><scope>7TM</scope><scope>7TN</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>F1W</scope><scope>FR3</scope><scope>H94</scope><scope>H95</scope><scope>K9.</scope><scope>L.G</scope><scope>M7N</scope><scope>P64</scope><scope>7X8</scope><scope>7S9</scope><scope>L.6</scope></search><sort><creationdate>20230401</creationdate><title>Thioredoxin A of Streptococcus suis Serotype 2 Contributes to Virulence by Inhibiting the Expression of Pentraxin 3 to Promote Survival Within Macrophages</title><author>Zhao, Chijun ; Jia, Xinglin ; Pan, Yanying ; Liao, Simeng ; Zhang, Shuo ; Ji, Chunxiao ; Kuang, Guangwei ; Wu, Xin ; Liu, Quan ; Tang, Yulong ; Fang, Lihua</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c408t-9b1d3a14356f7cc24fa27016e771581c8cbe6ec0dca12c7bf018d9fc22f450303</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2023</creationdate><topic>adhesion</topic><topic>Amino acids</topic><topic>Animals</topic><topic>antioxidants</topic><topic>Apoptosis</topic><topic>Bacteria</topic><topic>Bacterial Proteins - metabolism</topic><topic>Biomedical and Life Sciences</topic><topic>Cytotoxicity</topic><topic>Epithelial cells</topic><topic>Epithelium</topic><topic>Genes</topic><topic>Humans</topic><topic>Hydrogen peroxide</topic><topic>Hydrogen Peroxide - metabolism</topic><topic>Hydrogen Peroxide - pharmacology</topic><topic>Inflammation</topic><topic>Inflammatory response</topic><topic>Inoculation</topic><topic>Insulin</topic><topic>intestines</topic><topic>Life Sciences</topic><topic>liver</topic><topic>Macrophages</topic><topic>Macrophages - metabolism</topic><topic>Mice</topic><topic>Microbial Pathogenesis and Host-Microbe Interaction</topic><topic>Microbiology</topic><topic>Microorganisms</topic><topic>Mutants</topic><topic>Open reading frames</topic><topic>Oxidative stress</topic><topic>Oxidoreductions</topic><topic>Paraquat</topic><topic>Pathogenesis</topic><topic>Pathogenicity</topic><topic>Pathogens</topic><topic>Pentraxins</topic><topic>Phagocytes</topic><topic>phagocytosis</topic><topic>Recombinants</topic><topic>Serogroup</topic><topic>serotypes</topic><topic>Streptococcal Infections</topic><topic>Streptococcus infections</topic><topic>Streptococcus suis</topic><topic>Streptococcus suis - metabolism</topic><topic>Survival</topic><topic>Swine</topic><topic>temperature</topic><topic>Temperature tolerance</topic><topic>Thioredoxin</topic><topic>thioredoxins</topic><topic>Thioredoxins - genetics</topic><topic>Thioredoxins - metabolism</topic><topic>Thioredoxins - pharmacology</topic><topic>Virulence</topic><topic>Virulence - genetics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Zhao, Chijun</creatorcontrib><creatorcontrib>Jia, Xinglin</creatorcontrib><creatorcontrib>Pan, Yanying</creatorcontrib><creatorcontrib>Liao, Simeng</creatorcontrib><creatorcontrib>Zhang, Shuo</creatorcontrib><creatorcontrib>Ji, Chunxiao</creatorcontrib><creatorcontrib>Kuang, Guangwei</creatorcontrib><creatorcontrib>Wu, Xin</creatorcontrib><creatorcontrib>Liu, Quan</creatorcontrib><creatorcontrib>Tang, Yulong</creatorcontrib><creatorcontrib>Fang, Lihua</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Nucleic Acids Abstracts</collection><collection>Oceanic Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><collection>AGRICOLA</collection><collection>AGRICOLA - Academic</collection><jtitle>The journal of microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zhao, Chijun</au><au>Jia, Xinglin</au><au>Pan, Yanying</au><au>Liao, Simeng</au><au>Zhang, Shuo</au><au>Ji, Chunxiao</au><au>Kuang, Guangwei</au><au>Wu, Xin</au><au>Liu, Quan</au><au>Tang, Yulong</au><au>Fang, Lihua</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Thioredoxin A of Streptococcus suis Serotype 2 Contributes to Virulence by Inhibiting the Expression of Pentraxin 3 to Promote Survival Within Macrophages</atitle><jtitle>The journal of microbiology</jtitle><stitle>J Microbiol</stitle><addtitle>J Microbiol</addtitle><date>2023-04-01</date><risdate>2023</risdate><volume>61</volume><issue>4</issue><spage>433</spage><epage>448</epage><pages>433-448</pages><issn>1225-8873</issn><eissn>1976-3794</eissn><abstract>Streptococcus suis
serotype 2 (SS2) is an important zoonotic pathogen that can infect humans in contact with infected pigs or their byproducts. It can employ different types of genes to defend against oxidative stress and ensure its survival. The thioredoxin (Trx) system is a key antioxidant system that contributes adversity adaptation and pathogenicity. SS2 has been shown to encode putative thioredoxin genes, but the biological roles, coding sequence, and underlying mechanisms remains uncharacterized. Here, we demonstrated that SSU05_0237-ORF, from a clinical SS2 strain, ZJ081101, encodes a protein of 104 amino acids with a canonical CGPC active motif and an identity 70–85% similar to the thioredoxin A (TrxA) in other microorganisms. Recombinant TrxA efficiently catalyzed the thiol-disulfide oxidoreduction of insulin. The deletion of TrxA led to a significantly slow growth and markedly compromised tolerance of the pathogen to temperature stress, as well as impaired adhesion ability to pig intestinal epithelial cells (IPEC-J2). However, it was not involved in H
2
O
2
and paraquat-induced oxidative stress. Compared with the wild-type strain, the ΔTrxA strain was more susceptible to killing by macrophages through increasing NO production. Treatment with TrxA mutant strain also significantly attenuated cytotoxic effects on RAW 264.7 cells by inhibiting inflammatory response and apoptosis. Knockdown of pentraxin 3 in RAW 264.7 cells was more vulnerable to phagocytic activity, and TrxA promoted SS2 survival in phagocytic cells depending on pentraxin 3 activity compared with the wild-type strain. Moreover, a co-inoculation experiment in mice revealed that TrxA mutant strain is far more easily cleared from the body than the wild type strain in the period from 8–24 h, and exhibits significantly attenuated oxidative stress and liver injury. In summary, we reveal the important role of TrxA in the pathogenesis of SS2.</abstract><cop>Seoul</cop><pub>The Microbiological Society of Korea</pub><pmid>37010796</pmid><doi>10.1007/s12275-023-00038-4</doi><tpages>16</tpages></addata></record> |
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source | Springer Nature |
subjects | adhesion Amino acids Animals antioxidants Apoptosis Bacteria Bacterial Proteins - metabolism Biomedical and Life Sciences Cytotoxicity Epithelial cells Epithelium Genes Humans Hydrogen peroxide Hydrogen Peroxide - metabolism Hydrogen Peroxide - pharmacology Inflammation Inflammatory response Inoculation Insulin intestines Life Sciences liver Macrophages Macrophages - metabolism Mice Microbial Pathogenesis and Host-Microbe Interaction Microbiology Microorganisms Mutants Open reading frames Oxidative stress Oxidoreductions Paraquat Pathogenesis Pathogenicity Pathogens Pentraxins Phagocytes phagocytosis Recombinants Serogroup serotypes Streptococcal Infections Streptococcus infections Streptococcus suis Streptococcus suis - metabolism Survival Swine temperature Temperature tolerance Thioredoxin thioredoxins Thioredoxins - genetics Thioredoxins - metabolism Thioredoxins - pharmacology Virulence Virulence - genetics |
title | Thioredoxin A of Streptococcus suis Serotype 2 Contributes to Virulence by Inhibiting the Expression of Pentraxin 3 to Promote Survival Within Macrophages |
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