The effectiveness of extended binding affinity of prophage lysin PlyARI against Streptococcus suis infection
Streptococcus suis is an important zoonotic pathogen. An increase in multi-drug-resistant strains has led to poor performance of traditional antibiotic therapies. Thus, alternative antibacterial agents are urgently needed. In this study, we identified a recombined and expressed lysin PlyARI derived...
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Veröffentlicht in: | Archives of microbiology 2021-10, Vol.203 (8), p.5163-5172 |
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creator | Xiao, Yuyi Chen, Rong Li, Min Qi, Zitai Yu, Yanfei Pan, Zihao Yao, Huochun Feng, Zhixin Zhang, Wei |
description | Streptococcus suis
is an important zoonotic pathogen. An increase in multi-drug-resistant strains has led to poor performance of traditional antibiotic therapies. Thus, alternative antibacterial agents are urgently needed. In this study, we identified a recombined and expressed lysin PlyARI derived from the novel serotype
S. suis
(
Chz
) prophage PhiARI0460–1. The recombinant PlyARI at a concentration of 10 µg/mL showed high bacteriolytic activity against 30
S. suis
isolates. The minimum inhibitory concentration (MIC) of PlyARI against
S. suis
was found to be as low as 2 µg/mL, and the lytic efficiency could be maintained between the range of pH 4 and 12. Additionally, in a mouse infection model, a dose of 0.5 mg of PlyARI protected 10 out of 10 mice that were challenged with highly virulent
S. suis
strain HA9801. Furthermore, the binding specificity of PlyARI was evaluated by constructing a green fluorescent protein (GFP-ARIb), where GFP was fused with the PlyARI-SH3b (cell wall-binding domain, CBD), revealing a high affinity to
S. suis
,
Staphylococcus aureus,
and
Streptococcus equi
along with exhibiting a medium affinity to
Streptococcus pneumoniae
as well as
Streptococcus agalactiae.
Overall, our findings indicated that PlyARI may be an alternative antibacterial agent that was useful in treating and possibly the prevention of Streptococcal infections. |
doi_str_mv | 10.1007/s00203-021-02438-9 |
format | Article |
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is an important zoonotic pathogen. An increase in multi-drug-resistant strains has led to poor performance of traditional antibiotic therapies. Thus, alternative antibacterial agents are urgently needed. In this study, we identified a recombined and expressed lysin PlyARI derived from the novel serotype
S. suis
(
Chz
) prophage PhiARI0460–1. The recombinant PlyARI at a concentration of 10 µg/mL showed high bacteriolytic activity against 30
S. suis
isolates. The minimum inhibitory concentration (MIC) of PlyARI against
S. suis
was found to be as low as 2 µg/mL, and the lytic efficiency could be maintained between the range of pH 4 and 12. Additionally, in a mouse infection model, a dose of 0.5 mg of PlyARI protected 10 out of 10 mice that were challenged with highly virulent
S. suis
strain HA9801. Furthermore, the binding specificity of PlyARI was evaluated by constructing a green fluorescent protein (GFP-ARIb), where GFP was fused with the PlyARI-SH3b (cell wall-binding domain, CBD), revealing a high affinity to
S. suis
,
Staphylococcus aureus,
and
Streptococcus equi
along with exhibiting a medium affinity to
Streptococcus pneumoniae
as well as
Streptococcus agalactiae.
Overall, our findings indicated that PlyARI may be an alternative antibacterial agent that was useful in treating and possibly the prevention of Streptococcal infections.</description><identifier>ISSN: 0302-8933</identifier><identifier>EISSN: 1432-072X</identifier><identifier>DOI: 10.1007/s00203-021-02438-9</identifier><language>eng</language><publisher>Berlin/Heidelberg: Springer Berlin Heidelberg</publisher><subject>Affinity ; Antibacterial agents ; Antibiotics ; Antiinfectives and antibacterials ; Binding ; Biochemistry ; Biomedical and Life Sciences ; Biotechnology ; Cell Biology ; Cell walls ; Domain walls ; Drug resistance ; Ecology ; Fluorescence ; Green fluorescent protein ; Life Sciences ; Microbial Ecology ; Microbiology ; Minimum inhibitory concentration ; Original Paper ; Streptococcus infections ; Streptococcus suis</subject><ispartof>Archives of microbiology, 2021-10, Vol.203 (8), p.5163-5172</ispartof><rights>The Author(s), under exclusive licence to Springer-Verlag GmbH Germany, part of Springer Nature 2021</rights><rights>The Author(s), under exclusive licence to Springer-Verlag GmbH Germany, part of Springer Nature 2021.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c418t-7b068c15a913392cdd54c44179ee8b72100cddc58013a409eed62b3437f88d333</citedby><cites>FETCH-LOGICAL-c418t-7b068c15a913392cdd54c44179ee8b72100cddc58013a409eed62b3437f88d333</cites><orcidid>0000-0002-3575-6225</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s00203-021-02438-9$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00203-021-02438-9$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,27924,27925,41488,42557,51319</link.rule.ids></links><search><creatorcontrib>Xiao, Yuyi</creatorcontrib><creatorcontrib>Chen, Rong</creatorcontrib><creatorcontrib>Li, Min</creatorcontrib><creatorcontrib>Qi, Zitai</creatorcontrib><creatorcontrib>Yu, Yanfei</creatorcontrib><creatorcontrib>Pan, Zihao</creatorcontrib><creatorcontrib>Yao, Huochun</creatorcontrib><creatorcontrib>Feng, Zhixin</creatorcontrib><creatorcontrib>Zhang, Wei</creatorcontrib><title>The effectiveness of extended binding affinity of prophage lysin PlyARI against Streptococcus suis infection</title><title>Archives of microbiology</title><addtitle>Arch Microbiol</addtitle><description>Streptococcus suis
is an important zoonotic pathogen. An increase in multi-drug-resistant strains has led to poor performance of traditional antibiotic therapies. Thus, alternative antibacterial agents are urgently needed. In this study, we identified a recombined and expressed lysin PlyARI derived from the novel serotype
S. suis
(
Chz
) prophage PhiARI0460–1. The recombinant PlyARI at a concentration of 10 µg/mL showed high bacteriolytic activity against 30
S. suis
isolates. The minimum inhibitory concentration (MIC) of PlyARI against
S. suis
was found to be as low as 2 µg/mL, and the lytic efficiency could be maintained between the range of pH 4 and 12. Additionally, in a mouse infection model, a dose of 0.5 mg of PlyARI protected 10 out of 10 mice that were challenged with highly virulent
S. suis
strain HA9801. Furthermore, the binding specificity of PlyARI was evaluated by constructing a green fluorescent protein (GFP-ARIb), where GFP was fused with the PlyARI-SH3b (cell wall-binding domain, CBD), revealing a high affinity to
S. suis
,
Staphylococcus aureus,
and
Streptococcus equi
along with exhibiting a medium affinity to
Streptococcus pneumoniae
as well as
Streptococcus agalactiae.
Overall, our findings indicated that PlyARI may be an alternative antibacterial agent that was useful in treating and possibly the prevention of Streptococcal infections.</description><subject>Affinity</subject><subject>Antibacterial agents</subject><subject>Antibiotics</subject><subject>Antiinfectives and antibacterials</subject><subject>Binding</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Biotechnology</subject><subject>Cell Biology</subject><subject>Cell walls</subject><subject>Domain walls</subject><subject>Drug resistance</subject><subject>Ecology</subject><subject>Fluorescence</subject><subject>Green fluorescent protein</subject><subject>Life Sciences</subject><subject>Microbial Ecology</subject><subject>Microbiology</subject><subject>Minimum inhibitory concentration</subject><subject>Original Paper</subject><subject>Streptococcus infections</subject><subject>Streptococcus suis</subject><issn>0302-8933</issn><issn>1432-072X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNp9kdFLHDEQxkNpoVf1H_Ap4Etftp1ksib7KNLqgaBUBd9CLjt7RtbsubMrvf--Oa9Q6IMPITDz-z5m5hPiWME3BWC_M4AGrECr8gy6qvkgFsqgrsDqh49iAQi6cg3iZ_GF-QlAaefcQvR3jySp6yhO6ZUyMcuhk_R7otxSK1cptymvZei6lNO03TU347B5DGuS_ZZTljf99uzXUoZ1SJkneTuNtJmGOMQ4s-Q5sUz5zX7Ih-JTF3qmo7__gbj_-ePu_LK6ur5Ynp9dVdEoN1V2Bacuqjo0CrHRsW1rE41RtiFyK6vLxqUWawcKg4FSbU_1Cg3azrkWEQ_E171vGfVlJp78c-JIfR8yDTN7Xde2RlOOUNCT_9CnYR5zma5QDtDaRu0ovafiODCP1PnNmJ7DuPUK_C4Avw_AlwD8WwC-KSLci7jAeU3jP-t3VH8AFJWI9A</recordid><startdate>20211001</startdate><enddate>20211001</enddate><creator>Xiao, Yuyi</creator><creator>Chen, Rong</creator><creator>Li, Min</creator><creator>Qi, Zitai</creator><creator>Yu, Yanfei</creator><creator>Pan, Zihao</creator><creator>Yao, Huochun</creator><creator>Feng, Zhixin</creator><creator>Zhang, Wei</creator><general>Springer Berlin Heidelberg</general><general>Springer Nature B.V</general><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QL</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>RC3</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0002-3575-6225</orcidid></search><sort><creationdate>20211001</creationdate><title>The effectiveness of extended binding affinity of prophage lysin PlyARI against Streptococcus suis infection</title><author>Xiao, Yuyi ; Chen, Rong ; Li, Min ; Qi, Zitai ; Yu, Yanfei ; Pan, Zihao ; Yao, Huochun ; Feng, Zhixin ; Zhang, Wei</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c418t-7b068c15a913392cdd54c44179ee8b72100cddc58013a409eed62b3437f88d333</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2021</creationdate><topic>Affinity</topic><topic>Antibacterial agents</topic><topic>Antibiotics</topic><topic>Antiinfectives and antibacterials</topic><topic>Binding</topic><topic>Biochemistry</topic><topic>Biomedical and Life Sciences</topic><topic>Biotechnology</topic><topic>Cell Biology</topic><topic>Cell walls</topic><topic>Domain walls</topic><topic>Drug resistance</topic><topic>Ecology</topic><topic>Fluorescence</topic><topic>Green fluorescent protein</topic><topic>Life Sciences</topic><topic>Microbial Ecology</topic><topic>Microbiology</topic><topic>Minimum inhibitory concentration</topic><topic>Original Paper</topic><topic>Streptococcus infections</topic><topic>Streptococcus suis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Xiao, Yuyi</creatorcontrib><creatorcontrib>Chen, Rong</creatorcontrib><creatorcontrib>Li, Min</creatorcontrib><creatorcontrib>Qi, Zitai</creatorcontrib><creatorcontrib>Yu, Yanfei</creatorcontrib><creatorcontrib>Pan, Zihao</creatorcontrib><creatorcontrib>Yao, Huochun</creatorcontrib><creatorcontrib>Feng, Zhixin</creatorcontrib><creatorcontrib>Zhang, Wei</creatorcontrib><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Archives of microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Xiao, Yuyi</au><au>Chen, Rong</au><au>Li, Min</au><au>Qi, Zitai</au><au>Yu, Yanfei</au><au>Pan, Zihao</au><au>Yao, Huochun</au><au>Feng, Zhixin</au><au>Zhang, Wei</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The effectiveness of extended binding affinity of prophage lysin PlyARI against Streptococcus suis infection</atitle><jtitle>Archives of microbiology</jtitle><stitle>Arch Microbiol</stitle><date>2021-10-01</date><risdate>2021</risdate><volume>203</volume><issue>8</issue><spage>5163</spage><epage>5172</epage><pages>5163-5172</pages><issn>0302-8933</issn><eissn>1432-072X</eissn><abstract>Streptococcus suis
is an important zoonotic pathogen. An increase in multi-drug-resistant strains has led to poor performance of traditional antibiotic therapies. Thus, alternative antibacterial agents are urgently needed. In this study, we identified a recombined and expressed lysin PlyARI derived from the novel serotype
S. suis
(
Chz
) prophage PhiARI0460–1. The recombinant PlyARI at a concentration of 10 µg/mL showed high bacteriolytic activity against 30
S. suis
isolates. The minimum inhibitory concentration (MIC) of PlyARI against
S. suis
was found to be as low as 2 µg/mL, and the lytic efficiency could be maintained between the range of pH 4 and 12. Additionally, in a mouse infection model, a dose of 0.5 mg of PlyARI protected 10 out of 10 mice that were challenged with highly virulent
S. suis
strain HA9801. Furthermore, the binding specificity of PlyARI was evaluated by constructing a green fluorescent protein (GFP-ARIb), where GFP was fused with the PlyARI-SH3b (cell wall-binding domain, CBD), revealing a high affinity to
S. suis
,
Staphylococcus aureus,
and
Streptococcus equi
along with exhibiting a medium affinity to
Streptococcus pneumoniae
as well as
Streptococcus agalactiae.
Overall, our findings indicated that PlyARI may be an alternative antibacterial agent that was useful in treating and possibly the prevention of Streptococcal infections.</abstract><cop>Berlin/Heidelberg</cop><pub>Springer Berlin Heidelberg</pub><doi>10.1007/s00203-021-02438-9</doi><tpages>10</tpages><orcidid>https://orcid.org/0000-0002-3575-6225</orcidid></addata></record> |
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source | SpringerLink Journals - AutoHoldings |
subjects | Affinity Antibacterial agents Antibiotics Antiinfectives and antibacterials Binding Biochemistry Biomedical and Life Sciences Biotechnology Cell Biology Cell walls Domain walls Drug resistance Ecology Fluorescence Green fluorescent protein Life Sciences Microbial Ecology Microbiology Minimum inhibitory concentration Original Paper Streptococcus infections Streptococcus suis |
title | The effectiveness of extended binding affinity of prophage lysin PlyARI against Streptococcus suis infection |
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