Existence and characterization of allelic variants of Sao, a newly identified surface protein from Streptococcus suis

• Published in: FEMS Microbiology Letters 2007-10, Vol.275 (1), p.80-88
• Main Authors: Feng, Youjun, Zheng, Feng, Pan, Xiuzhen, Sun, Wen, Wang, Changjun, Dong, Yaqing, Ju, Ai-ping, Ge, Junchao, Liu, Di, Liu, Cuihua, Yan, Jinghua, Tang, Jiaqi, Gao, George F.
• Format: Article
• Language: English
• Subjects: Alleles; allelic variants; Amino Acid Sequence; Antibodies; antibody; Antigens; Antigens, Bacterial - analysis; Antigens, Bacterial - chemistry; Antigens, Bacterial - genetics; Antigens, Surface - genetics; Biological and medical sciences; ELISA; Enzyme-Linked Immunosorbent Assay; Fundamental and applied biological sciences. Psychology; Genes; Genes, Bacterial; Genetic Variation; Heterogeneity; M protein; Membrane Proteins - analysis; Membrane Proteins - chemistry; Membrane Proteins - genetics; Microbiology; Molecular Sequence Data; Monitoring methods; Pathogenesis; Pathogenicity; Pathogens; Proteins; Research Letters; Sao protein; Sequences; Streptococcus infections; Streptococcus suis; Streptococcus suis - genetics; Streptococcus suis - immunology
• ISSN: 0378-1097; 1574-6968
• DOI: 10.1111/j.1574-6968.2007.00859.x

Abstract Surface antigen one (Sao) is a newly identified protein from the major zoonotic pathogen, Streptococcus suis. In search of functional proteins related to the pathogenesis of Chinese S. suis 2 (SS2), unexpectedly, a variant of Sao protein was obtained. To test its prevalence in S. suis, PCR assay was adopted to address the coding genes systematically. It was found that there are three allelic variants of sao gene, namely sao-S, sao-M, and sao-L based on the different lengths of the genes (∼1.5, ∼1.7, and ∼2.0 kb, respectively). These differences were determined to be caused by heterogeneity within the number of C-terminal repeat sequences (R), which had been seen as a pathogenicity-related domain in the plant pathogen, Xanthomonas oryzae. Two variants (sao-M and sao-L) were only found in SS2. All three variant proteins were prepared in vitro and their biochemical and biophysical properties were characterized. A soluble form of Sao-M protein was then used as a capture antigen to develop an enzyme-linked immunosorbent assay method to detect antibodies against SS2 in convalescent pig sera. Taken together, the results exhibit the properties of Sao proteins and provide an efficient Sao-M-based method for monitoring SS2 infection.