MOLECULAR AND IMMUNOLOGICAL CHARACTERIZATION OF A 64-KDA PROTEIN OF ACTINOBACILLUS-ACTINOMYCETEMCOMITANS

被引：46

作者：

NAKANO, Y

INAI, Y

YAMASHITA, Y

NAGAOKA, S

KUSUZAKINAGIRA, T

NISHIHARA, T

OKAHASHI, N

KOGA, T

机构：

[1] KYUSHU UNIV, FAC DENT, DEPT PREVENT DENT, HIGASHI KU, FUKUOKA 812, JAPAN

[2] KAGOSHIMA UNIV, SCH DENT, DEPT OPERAT DENT & ENDODONTOL, KAGOSHIMA 890, JAPAN

[3] AICHI GAKUIN UNIV, SCH DENT, DEPT PERIODONTOL, NAGOYA, AICHI, JAPAN

[4] NATL INST HLTH, DEPT ORAL SCI, TOKYO 141, JAPAN

来源：

ORAL MICROBIOLOGY AND IMMUNOLOGY | 1995年 / 10卷 / 03期

关键词：

HEAT SHOCK PROTEIN; GROEL; HSP60; ACTINOBACILLUS ACTINOMYCETEMCOMITANS; PERIODONTITIS;

D O I：

10.1111/j.1399-302X.1995.tb00136.x

中图分类号：

R78 [口腔科学];

学科分类号：

1003 ;

摘要：

The 64-kDa protein to which about half the sera from patients with localized juvenile periodontitis and rapidly progressive periodontitis reacted strongly was purified from Actinobacillus actinomycetemcomitans Y4. Determination of the N-terminal sequence of the protein revealed that it was a GroEL-like protein. The DNA fragment containing the groEL gene of A. actinomycetemcomitans was amplified by polymerase chain reaction, and the groESL operon was cloned by using colony hybridization with the amplified fragment from A. actinomycetemcomitans chromosomal DNA. Sequence analysis revealed that structures of the operon and its products were typical in gram-negative bacteria. Rabbit polyclonal antibodies to the 64-kDa protein cross-reacted with approximately 65-kDa proteins of Haemophilus aphrophilus, Haemophilus influenzae, Haemophilus paraphrophilus, Escherichia coli and Eikenella corrodens but not with any cellular proteins of Porphyromonas gingivalis, Prevotella intermedia and Fusobacterium nucleatum. It is possible that antibodies reactive to the 64-kDa protein in periodontitis patients are induced by the cross-reactivity with the hsp60 proteins of other bacteria.

引用

页码：151 / 159

页数：9

共 33 条

[1]

Burnette WN., “Western blotting”: electrophoretic transfer of proteins from sodium dodecyl sulfate‐polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A, Anal Biochem, 112, pp. 195-203, (1981)

[2]

Burns DL, Gould-Kostka JL, Kessel M, Arciniega JL., Purification and immunological characterization of a GroEL‐like protein from Bordetella pertussis, Infect Immun, 59, pp. 1417-1422, (1991)

[3]

Cowing DW, Bardwell JCA, Craig EA, Woolford C, Hendrix RR, Cross CA., Consensus sequence for Escherichia coli heat shock gene promoters, Proc Natl Acad Sci U S A, 82, pp. 2679-2683, (1985)

[4]

Grenier D, Chao C, McBride BC., Characterization of sodium dodecyl sulfate‐stable Bacteroides gingivalis proteases by polyacrylamide gel electrophoresis, Infect Immun, 57, pp. 95-99, (1989)

[5]

Hemmingsen SM, Woolford C, van der Vies SM, Et al., Homologous plant and bacterial proteins chaperone oligomeric protein assembly, Nature, 333, pp. 330-334, (1988)

[6]

Hinode D, Hayashi H, Nakamura R., Purification and characterization of three types of proteases from culture supernatants of Porphyromonas gingivalis, Infect Immun, 59, pp. 3060-3068, (1991)

[7]

Jindal S, Dudani AK, Singh B, Harley CB, Gupta RS., Primary structure of a human mitochondrial protein homologous to the bacterial and plant chaperonins and to the 65‐kilodalton mycobacterial antigen, Mol Cell Biol, 9, pp. 2279-2283, (1989)

[8]

Kaplan AH, Weber DJ, Oddone EZ, Perfect JR., Infection due to Actinobacillus actinomycetemcomitans: 15 cases and review, Rev Infect Dis, 11, pp. 46-63, (1989)

[9]

Kiessling R, Gronberg A, Ivanyi J, Et al., Role of hsp60 during autoimmune and bacterial inflammation, Immunological Reviews, 121, pp. 91-111, (1991)

[10]

Koga T, Kusuzaki T, Asakawa H, Senpuku H, Nishihara T, Noguchi T., The 64‐kilodalton GroEL‐like protein of Actinobacillus actinomycetemcomitans, J Periodont Res, 28, pp. 475-477, (1993)

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