Characterization of LppS, an adhesin of Mycoplasma conjunctivae
Characterization of LppS, an adhesin of Mycoplasma conjunctivae
复制标题
DOI：
10.1099/mic.0.25864-0
复制
发表时间：
2003-01-01
期刊：
影响因子：
2.8
通讯作者：
Frey, J
中科院分区：
文献类型：
--
作者：
Belloy, L;Vilei, EM;Frey, J
结膜支原体是引起山羊科传染性角膜结膜炎（IKC）的病原体，其膜蛋白富含丝氨酸，命名为LppS。基因克隆和序列分析表明，它编码的膜蛋白前体。该蛋白具有典型的信号序列和信号肽酶II裂解位点，随后是代表潜在酰化位点的半胱氨酸残基。成熟LppS蛋白的表观分子量为150 kDa，存在于吐温20提取的M.结膜蛋白。它具有一个富含丝氨酸的结构域，由41个氨基酸组成，其中37个（90.2%）为丝氨酸残基。这些丝氨酸残基中的27个是连续的。该蛋白粘附于羊关节滑膜细胞。使用体外粘附模型，来自IgG的针对重组纯化LppS的Fab片段显示特异性抑制M的粘附。结膜到羔羊细胞。因此，LppS可能是M.可能在IKC的发病机制中起重要作用。
A serine-rich membrane protein named LppS from Mycoplasma conjunctivae, the aetiological agent of infectious keratoconjunctivitis (IKC) of domestic and wild Caprinae, was characterized. Gene cloning and sequence analysis of the IppS gene revealed that it encoded a membrane protein precursor. The protein had a typical signal sequence and a signal peptidase II cleavage site followed by a cysteine residue representing a potential acylation site. The mature LppS protein had an apparent molecular mass of 150 kDa and was found in the detergent-associated fraction of Tween 20 extracted M. conjunctivae proteins. It possessed a serine-rich domain of 41 aa with 37 (90.2%) serine residues. Twenty-seven of these serine residues were contiguous. The protein adhered to lamb joint synovial cells. Using an in vitro adhesion model, Fab fragments from IgG directed against recombinant purified LppS were shown to specifically inhibit adhesion of M. conjunctivae to lamb cells. Thus, LppS is likely to be an adhesin of M. conjunctivae that may play an important role in the pathogenesis of IKC.