IMMUNOBIOLOGICAL ACTIVITIES OF SYNTHETIC PEPTIDE SEGMENTS OF FIMBRIAL PROTEIN FROM PORPHYROMONAS-GINGIVALIS

被引：60

作者：

OGAWA, T ^{[1
]}

KUSUMOTO, Y ^{[1
]}

UCHIDA, H ^{[1
]}

NAGASHIMA, S ^{[1
]}

OGO, H ^{[1
]}

HAMADA, S ^{[1
]}

机构：

[1] OSAKA UNIV,FAC DENT,DEPT ORAL MICROBIOL,SUITA,OSAKA 565,JAPAN

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1991年 / 180卷 / 03期

关键词：

D O I：

10.1016/S0006-291X(05)81342-7

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Several oligopeptide segments of fimbrial subunit protein (fimbrilin) of Porphyromonas gingivalis strain 381 were synthesized and tested for immunobiological activities. Peptides F3(31-50; amino acid residue numbers 31 to 50, based on the amino acid sequence of the fimbrilin proposed by Dickinson et al., Infect. Immun., 170, 1658, 1988), F12(212-231) and F17(312-331) were found to be immunodominant epitopes of this fimbrial protein as revealed by ELISA. Furthermore, peptides F5(71-90) and F17(312-331) were demonstrated to agglutinate rabbit erythrocytes, and were mitogenic for BALB/c spleen cells but not thymocytes. These peptides enhanced the number of fimbria-specific antibody-secreting cells in BALB/c spleen cell cultures, and induced cytokines such as tumor necrosis factor-alpha and interleukin-6 production in human monocyte/macrophage cultures. The data demonstrate that these defined peptide segments are responsible for the immunostimulating portions within the fimbrial protein molecule. © 1991 Academic Press, Inc.

引用

页码：1335 / 1341

页数：7

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