A novel, anchorless streptococcal surface protein that binds to human immunoglobulins
A novel, anchorless streptococcal surface protein that binds to human immunoglobulins
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DOI：
10.1016/s0006-291x(02)02078-8
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发表时间：
2002-09-06
影响因子：
3.1
通讯作者：
Hamada, S
中科院分区：
文献类型：
--
作者：
Kawabata, S;Tamura, Y;Hamada, S
我们从a群化脓性链球菌（GAS）全细胞尿素提取物中鉴定了一种新的表面蛋白。Western blotting检测到一个主要的蛋白带（35kd）与人IgG杂交。利用GAS基因组序列数据库搜索该蛋白的n端氨基酸序列，发现一个开放的阅读框编码一个38kda的蛋白和一个信号肽序列。我们将该蛋白命名为链球菌免疫球蛋白结合蛋白35 （Sib35）。它是一种不含LPXTG基序的无锚蛋白，与具有免疫球蛋白结合活性的M蛋白超家族不同，部分分泌于培养上清中。重组Sib35也被证明能结合人IgA和IgM。sib35基因在所有检测的GAS菌株中均被发现，但在口服、B、C或G组链球菌菌株中未被发现。这些结果表明，Sib35是GAS中独特的免疫球蛋白结合蛋白。(C) 2002 Elsevier Science （USA）。版权所有。
We have characterized a novel surface protein from urea extract of whole cells of group A Streptococcus pyogenes (GAS). A major protein band (35 kD) was found to hybridize with human IgG by Western blotting. A search of the N-terminal amino acid sequence of this protein by using the GAS genome sequence database revealed an open reading frame that encoded a 38-kDa protein with a signal peptide sequence. We have named this protein streptococcal immunoglobulin-binding protein 35 (Sib35). It was found to be an anchorless protein with no LPXTG motif, distinct from the M protein superfamily exhibiting immunoglobulin-binding activity, and partially secreted in the culture supernatant. Recombinant Sib35 was also shown to bind human IgA and IgM. The sib35 gene was found in all GAS strains examined, but not in oral, group B, C, or G streptococcal strains. These results suggest that Sib35 is a unique immunoglobulin-binding protein in GAS. (C) 2002 Elsevier Science (USA). All rights reserved.