TY - JOUR
T1 - Molecular and immunological characterization of a 64‐kDa protein of Actinobacillus actinomycetemcomitans
AU - Nakano, Y.
AU - Inai, Y.
AU - Yamashita, Y.
AU - Nagaoka, S.
AU - Kusuzaki‐Nagira, T.
AU - Nishihara, T.
AU - Okahashi, N.
AU - Koga, T.
PY - 1995/6
Y1 - 1995/6
N2 - 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 TV‐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 Fusobacteriuni 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.
AB - 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 TV‐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 Fusobacteriuni 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.
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U2 - 10.1111/j.1399-302X.1995.tb00136.x
DO - 10.1111/j.1399-302X.1995.tb00136.x
M3 - Article
C2 - 7567064
AN - SCOPUS:0029311224
SN - 0902-0055
VL - 10
SP - 151
EP - 159
JO - Oral Microbiology and Immunology
JF - Oral Microbiology and Immunology
IS - 3
ER -