Beachey E H, Seyer J M
J Immunol. 1986 Mar 15;136(6):2287-92.
The protective immunogenicity of chemically synthesized copies of the NH2-terminal region of type 6 streptococcal M protein was investigated. Four overlapping peptides were synthesized by copying residues 1-20, 10-20, 12-31, and 22-31. Rabbit antisera raised against whole cells of type 6 streptococci reacted at high dilutions (1/12,800 to 1/51,200) with S-M6(1-20) and S-M6(10-20), and at low dilutions (1/100-1/800) with S-M6(12-31) and S-M6(22-31), indicating that the NH2-terminal region of type 6 M protein bears immunodominant epitopes. When covalently linked to tetanus toxoid and emulsified in complete Freund's adjuvant, the synthetic peptides S-M6(1-20), S-M6(10-20), and S-M6(12-31), but not S-M6(22-31), evoked type-specific opsonic antibodies against type 6 streptococci. Although the immune sera reacted in low dilutions by enzyme linked immunoabsorbent assay (ELISA) with the heterologous M protein polypeptides pep M5, pep M19, and pep M24, they failed to opsonize the streptococci from which these M protein polypeptides were derived. Each of the immune sera reacted in high dilution by ELISA with the respective immunizing peptides. All except those against S-M6(22-31) also reacted with pep M6. None of the immune sera reacted with human cardiac tissue by immunofluorescence or with muscle myosin by ELISA. The pattern of the inhibition of opsonization by each of the synthetic peptides of each of the immune sera indicates the presence of at least three protective epitopes in the NH2-terminal region of type 6 M protein. Our results indicate that the NH2-terminal region of type 6 M protein contains both protective and nonprotective epitopes, and chemically synthesized copies of this region lack cardiac tissue cross-reactive epitopes. These studies hold promise for the development of safe and effective vaccines against group A streptococci, especially against the strains giving rise to rheumatic fever and rheumatic heart disease.
研究了6型链球菌M蛋白氨基末端区域化学合成拷贝的保护性免疫原性。通过复制第1 - 20、10 - 20、12 - 31和22 - 31位残基合成了四种重叠肽。用6型链球菌全细胞免疫兔产生的抗血清,在高稀释度(1/12,800至1/51,200)下与S - M6(1 - 20)和S - M6(10 - 20)反应,在低稀释度(1/100 - 1/800)下与S - M6(12 - 31)和S - M6(22 - 31)反应,表明6型M蛋白的氨基末端区域具有免疫显性表位。当与破伤风类毒素共价连接并乳化于完全弗氏佐剂中时,合成肽S - M6(1 - 20)、S - M6(10 - 20)和S - M6(12 - 31),而非S - M6(22 - 31),诱发了针对6型链球菌的型特异性调理抗体。尽管免疫血清通过酶联免疫吸附测定(ELISA)在低稀释度下与异源M蛋白多肽pep M5、pep M19和pep M24反应,但它们未能调理产生这些M蛋白多肽的链球菌。每种免疫血清通过ELISA在高稀释度下与各自的免疫肽反应。除了针对S - M6(22 - 31)的那些血清外,所有血清也与pep M6反应。没有一种免疫血清通过免疫荧光与人心脏组织反应,也没有通过ELISA与肌肉肌球蛋白反应。每种免疫血清的每种合成肽对调理作用的抑制模式表明,6型M蛋白氨基末端区域存在至少三个保护性表位。我们的结果表明,6型M蛋白的氨基末端区域既包含保护性表位也包含非保护性表位,并且该区域的化学合成拷贝缺乏心脏组织交叉反应性表位。这些研究为开发安全有效的抗A组链球菌疫苗,尤其是针对引起风湿热和风湿性心脏病的菌株的疫苗带来了希望。