Candida albicans binding to the oral bacterium Streptococcus gordonii involves multiple adhesin-receptor interactions
Candida albicans binding to the oral bacterium Streptococcus gordonii involves multiple adhesin-receptor interactions
复制标题
DOI：
10.1128/iai.64.11.4680-4685.1996
复制
发表时间：
1996-11-01
影响因子：
3.1
通讯作者：
Jenkinson, HF
中科院分区：
文献类型：
--
作者：
Holmes, AR;McNab, R;Jenkinson, HF
白色念珠菌通过识别链球菌细胞壁多糖受体与多种口腔链球菌，特别是戈登链球菌结合（A. R. Holmes、P. K. Gopal 和 H. F. Jenkinson，Infect. Immun. 63：1827-1834，1995），我们现在表明，戈登链球菌的同基因细胞表面蛋白突变体DL1 的细胞壁多糖表达不变，在固相测定中支持白色念珠菌细胞粘附的能力降低。编码高分子质量细胞表面多肽的戈氏沙门氏菌 cshA 和 cshB 基因失活，以及编码抗原 I/II 唾液粘附素的 sspA 和 sspB 基因失活，导致粘附能力分别降低 40% 和 79%白色念珠菌细胞，编码细胞表面脂蛋白的戈氏沙门氏菌 scaA 基因失活对白色念珠菌粘附没有影响，链球菌抗原 I/II 蛋白 SpaP 的多克隆抗血清和 CshA 氨基末端非重复 (NR) 结构域特异性抗体均抑制白色念珠菌与戈氏念珠菌细胞的粘附，相反，针对氨基酸重复序列的抗体阻断重复CshA的(R)结构域或ScaA的结构域不抑制白色念珠菌粘附。包含NR结构域或R结构域序列的CshA的固定化重组多肽片段均支持白色念珠菌细胞的粘附。粪肠球菌表面表达的戈登沙门氏菌 SspB 蛋白赋予肠球菌细胞结合白色念珠菌的能力，而抗原 I/II 抗血清可消除这种能力。总的来说，结果表明白色念珠菌与戈登沙门氏菌的相互作用是由粘附素-受体相互作用的补充介导的，该相互作用涉及链球菌多功能多肽粘附素、细菌细胞壁多糖和尚未鉴定的酵母细胞表面成分的两个家族。
Candida albicans binds to several species of oral streptococci, in particular Streptococcus gordonii, through recognition of a streptococcal cell wall polysaccharide receptor (A. R. Holmes, P. K. Gopal, and H. F. Jenkinson, Infect. Immun. 63:1827-1834, 1995), We now show that isogenic cell surface protein mutants of S. gordonii DL1, unaltered in expression of cell wall polysaccharide, are reduced in ability to support adherence of C. albicans cells in a solid-phase assay, Inactivation of the S. gordonii cshA and cshB genes, encoding high molecular-mass cell surface polypeptides, and inactivation of the sspA and sspB genes, encoding antigen I/II salivary adhesins, resulted in 40 and 79% reductions, respectively, in adherence of C. albicans cells, Inactivation of the S. gordonii scaA gene encoding a cell surface lipoprotein had no effect on C. albicans adherence, Polyclonal antiserum to streptococcal antigen I/II protein SpaP and antibodies specific to the amino-terminal nonrepetitive (NR) domain of CshA both inhibited adherence of C. albicans to S. gordonii cells, Conversely antibodies to the amino acid repeat block repetitive (R) domain of CshA or to ScaA, did not inhibit C. albicans adherence, Immobilized recombinant polypeptide fragments of CshA comprising NR domain or R domain sequences both supported adherence of C. albicans cells. Expression of S. gordonii SspB protein on the surface of Enterococcus faecalis conferred on the enterococcal cells the ability to bind C. albicans, and this was ablated by antigen I/II antiserum. Collectively the results suggest that interaction of C. albicans with S. gordonii is mediated by a complement of adhesin-receptor interactions that involves two families of streptococcal multifunctional polypeptide adhesins, bacterial cell wall polysaccharide, and as yet unidentified yeast cell surface components.