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细菌IgA1蛋白酶对恒河猴免疫球蛋白A（IgA）的切割缺失。

Lack of cleavage of immunoglobulin A (IgA) from rhesus monkeys by bacterial IgA1 proteases.

作者信息

Reinholdt J, Kilian M

机构信息

Department of Oral Biology, Royal Dental College Arhus, Denmark.

出版信息

Infect Immun. 1991 Jun;59(6):2219-21. doi: 10.1128/iai.59.6.2219-2221.1991.

DOI:10.1128/iai.59.6.2219-2221.1991
PMID:2037384
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC257993/
Abstract

Bacterial immunoglobulin A1 (IgA1) proteases cleaving IgA1 and secretory IgA1 molecules in the hinge region are believed to be important virulence factors. Previous studies have indicated that IgA of humans, gorillas, and chimpanzees are the exclusive substrates of these enzymes. In a recent study, IgA from the rhesus monkey was found to be susceptible to the IgA1 protease activity of Streptococcus pneumoniae. In an attempt to reproduce this observation, we found that neither five isolates of S. pneumoniae nor other IgA1 protease-producing bacteria representing different cleavage specificities caused cleavage of rhesus monkey IgA. Hence, the rhesus monkey does not appear to be a suitable animal model for studies of IgA1 proteases as virulence factors.

摘要

切割铰链区免疫球蛋白A1（IgA1）和分泌型IgA1分子的细菌IgA1蛋白酶被认为是重要的毒力因子。先前的研究表明，人类、大猩猩和黑猩猩的IgA是这些酶的唯一底物。在最近一项研究中，恒河猴的IgA被发现易受肺炎链球菌IgA1蛋白酶活性的影响。为了重现这一观察结果，我们发现五株肺炎链球菌分离株以及代表不同切割特异性的其他产生IgA1蛋白酶的细菌均未导致恒河猴IgA的切割。因此，恒河猴似乎不是研究作为毒力因子的IgA1蛋白酶的合适动物模型。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dfb2/257993/3d86700b008f/iai00042-0358-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dfb2/257993/3d86700b008f/iai00042-0358-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dfb2/257993/3d86700b008f/iai00042-0358-a.jpg

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