猪链球菌免疫球蛋白- g结合蛋白的检测。

B Serhir, R Higgins, B Foiry, M Jacques
{"title":"猪链球菌免疫球蛋白- g结合蛋白的检测。","authors":"B Serhir,&nbsp;R Higgins,&nbsp;B Foiry,&nbsp;M Jacques","doi":"10.1099/00221287-139-12-2953","DOIUrl":null,"url":null,"abstract":"<p><p>This study was undertaken to search for the presence of immunoglobulin G (IgG)-binding proteins in Streptococcus suis, an important swine pathogen. Whole bacterial cells were incubated with human or pig IgG conjugated to gold particles and examined by transmission electron microscopy. Cells of some S. suis strains were labelled as were cells of the positive control strain, Staphylococcus aureus Cowan I. Binding of pig and human IgG to five different bacterial species of group D streptococci, to reference strains representing the 29 capsular types of S. suis, and to 12 S. suis capsular type 2 strains was then examined using Western blotting. All strains interacted with pig and human IgG, although the binding profiles were slightly different. A 52 kDa protein was observed in all capsular types of S. suis. This protein, absent in other group D streptococcal species, was observed in all capsular type 2 isolates originating from diseased or clinically healthy pigs, and was shown to bind human IgG-Fc fragments. The IgG-binding activity was also observed in the culture supernatant and was sensitive to proteolysis.</p>","PeriodicalId":15884,"journal":{"name":"Journal of general microbiology","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"1993-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1099/00221287-139-12-2953","citationCount":"29","resultStr":"{\"title\":\"Detection of immunoglobulin-G-binding proteins in Streptococcus suis.\",\"authors\":\"B Serhir,&nbsp;R Higgins,&nbsp;B Foiry,&nbsp;M Jacques\",\"doi\":\"10.1099/00221287-139-12-2953\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>This study was undertaken to search for the presence of immunoglobulin G (IgG)-binding proteins in Streptococcus suis, an important swine pathogen. Whole bacterial cells were incubated with human or pig IgG conjugated to gold particles and examined by transmission electron microscopy. Cells of some S. suis strains were labelled as were cells of the positive control strain, Staphylococcus aureus Cowan I. Binding of pig and human IgG to five different bacterial species of group D streptococci, to reference strains representing the 29 capsular types of S. suis, and to 12 S. suis capsular type 2 strains was then examined using Western blotting. All strains interacted with pig and human IgG, although the binding profiles were slightly different. A 52 kDa protein was observed in all capsular types of S. suis. This protein, absent in other group D streptococcal species, was observed in all capsular type 2 isolates originating from diseased or clinically healthy pigs, and was shown to bind human IgG-Fc fragments. The IgG-binding activity was also observed in the culture supernatant and was sensitive to proteolysis.</p>\",\"PeriodicalId\":15884,\"journal\":{\"name\":\"Journal of general microbiology\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1993-12-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1099/00221287-139-12-2953\",\"citationCount\":\"29\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of general microbiology\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1099/00221287-139-12-2953\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of general microbiology","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1099/00221287-139-12-2953","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 29

摘要

本研究旨在寻找猪链球菌(一种重要的猪病原体)中免疫球蛋白G (IgG)结合蛋白的存在。整个细菌细胞与人或猪IgG结合金颗粒孵育,透射电镜检查。将部分猪链球菌的细胞标记为阳性对照菌株金黄色葡萄球菌(Staphylococcus aureus Cowan i)的细胞,用Western blotting检测猪和人IgG与5种不同的D组链球菌、29种猪链球菌荚膜型参考菌株和12种猪链球菌荚膜2型菌株的结合情况。所有菌株都与猪和人IgG相互作用,尽管结合谱略有不同。在所有猪链球菌荚膜类型中均检测到52 kDa蛋白。这种蛋白在其他D组链球菌中不存在,但在所有来自患病猪或临床健康猪的荚膜2型分离株中都观察到,并被证明能结合人IgG-Fc片段。在培养上清中也观察到igg结合活性,并且对蛋白质水解敏感。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
查看原文
分享 分享
微信好友 朋友圈 QQ好友 复制链接
本刊更多论文
Detection of immunoglobulin-G-binding proteins in Streptococcus suis.

This study was undertaken to search for the presence of immunoglobulin G (IgG)-binding proteins in Streptococcus suis, an important swine pathogen. Whole bacterial cells were incubated with human or pig IgG conjugated to gold particles and examined by transmission electron microscopy. Cells of some S. suis strains were labelled as were cells of the positive control strain, Staphylococcus aureus Cowan I. Binding of pig and human IgG to five different bacterial species of group D streptococci, to reference strains representing the 29 capsular types of S. suis, and to 12 S. suis capsular type 2 strains was then examined using Western blotting. All strains interacted with pig and human IgG, although the binding profiles were slightly different. A 52 kDa protein was observed in all capsular types of S. suis. This protein, absent in other group D streptococcal species, was observed in all capsular type 2 isolates originating from diseased or clinically healthy pigs, and was shown to bind human IgG-Fc fragments. The IgG-binding activity was also observed in the culture supernatant and was sensitive to proteolysis.

求助全文
通过发布文献求助,成功后即可免费获取论文全文。 去求助
来源期刊
自引率
0.00%
发文量
0
期刊最新文献
Partial protection against genital reinfection by immunization of guinea-pigs with isolated outer-membrane proteins of the chlamydial agent of guinea-pig inclusion conjunctivitis. Calcineurin-dependent growth of an FK506- and CsA-hypersensitive mutant of Saccharomyces cerevisiae. Typing of Clostridium difficile strains by PCR-amplification of variable length 16S-23S rDNA spacer regions. Antimicrobial activity and biosynthesis of indole antibiotics produced by Xenorhabdus nematophilus. Cloning and characterization of a tryptophanase gene from Enterobacter aerogenes SM-18.
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
现在去查看 取消
×
提示
确定
0
微信
客服QQ
Book学术公众号 扫码关注我们
反馈
×
意见反馈
请填写您的意见或建议
请填写您的手机或邮箱
已复制链接
已复制链接
快去分享给好友吧!
我知道了
×
扫码分享
扫码分享
Book学术官方微信
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术
文献互助 智能选刊 最新文献 互助须知 联系我们:info@booksci.cn
Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。
Copyright © 2023 Book学术 All rights reserved.
ghs 京公网安备 11010802042870号 京ICP备2023020795号-1