Identification and characterisation of hyaluronate lyase from Streptococcus suis
Identification and characterisation of hyaluronate lyase from Streptococcus suis
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DOI：
10.1016/j.micpath.2004.02.006
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发表时间：
2004-06-01
影响因子：
3.8
通讯作者：
Maskell, DJ
中科院分区：
文献类型：
--
作者：
Allen, AG;Lindsay, H;Maskell, DJ
透明质酸裂解酶催化透明质酸（HA）的降解，已被描述从几个致病性链球菌物种。我们描述。首次从人畜共患病猪链球菌中分离纯化了透明质酸裂解酶。我们克隆了S. suis的突变体，并利用其产生S.猪血清型7不再能生物合成酶。有趣的是，有限的菌株调查表明，透明质酸裂解酶活性并不存在于所有的疾病分离的S。猪。针对我们的重组透明质酸裂解酶产生的多克隆抗透明质酸裂解酶抗血清已用于蛋白质印迹，表明透明质酸裂解酶活性总是与预期大小的蛋白质的存在相关，而缺乏透明质酸裂解酶活性是由于酶的截短或不存在。我们发现透明质酸裂解酶活性是S。suis使用HA聚合物作为碳源，并向所有S.测试的猪菌株允许发酵所得HA分解产物。(C)2004爱思唯尔有限公司保留所有权利。
Hyaluronate lyase, which catalyses the degradation of hyaluronic acid (HA), has been described from several pathogenic streptococcal species. We describe. for the first time, identification and purification of hyaluronate lyase from the zoonotic pig pathogen Streptococcus suis. We have cloned the hyaluronate lyase gene from S. suis and used it to generate an allelic replacement knock-out mutant of S. suis serotype 7 that can no longer biosynthesise the enzyme. Interestingly, a limited strain survey indicates that hyaluronate lyase activity is not present in all disease isolates of S. suis. Polyclonal anti-hyaluronate lyase anti-serum raised against our recombinant hyaluronate lyase has been used in Western blots, showing that hyaluronate lyase activity is always associated with the presence of protein of the expected size, whereas lack of hyaluronate lyase activity is due to truncation or absence of the enzyme. We show that hyaluronate lyase activity is required for S. suis to use HA polymer as a carbon Source and that supplying exogenous recombinant hyaluronate lyase to all S. suis strains tested allowed fermentation of the resultant HA breakdown products. (C) 2004 Elsevier Ltd. All rights reserved.