Affiliation:
1. Department of Oral Biology, School of Dental Medicine, University at Buffalo, The State University of New York, Buffalo, New York 14214
Abstract
ABSTRACT
Salivary amylase binds specifically to a number of oral streptococcal species. This interaction may play an important role in dental plaque formation. Recently, a 585-bp gene was cloned and sequenced from
Streptococcus gordonii
Challis encoding a 20.5-kDa amylase-binding protein (AbpA). The goal of this study was to determine if related genes are present in other species of oral streptococci. Biotinylated
abpA
was used in Southern blot analysis to screen genomic DNA from several strains representing eight species of oral streptococci. This probe hybridized with a 4.0-kb
Hin
dIII restriction fragment from all 13 strains of
S. gordonii
tested. The probe did not appear to bind to any restriction fragments from other species of amylase-binding oral streptococci including
Streptococcus mitis
(with the exception of 1 of 14 strains),
Streptococcus crista
(3 strains),
Streptococcus anginosus
(1 strain), and
Streptococcus parasanguinis
(1 strain), or to non-amylase-binding oral streptococci including
Streptococcus sanguinis
(3 strains),
Streptococcus oralis
(4 strains), and
Streptococcus mutans
(1 strain). Primers homologous to sequences within the 3′ and 5′ ends of
abpA
yielded products of 400 bp following PCR of genomic DNA from the Southern blot-positive strains. Several of these PCR products were cloned and sequenced. The levels of similarity of these cloned products to the
abpA
of
S. gordonii
Challis ranged from 91 to 96%. These studies reveal that the
abpA
gene appears to be specific to
S. gordonii
and differs from genes encoding amylase-binding proteins from other species of amylase-binding streptococci.
Publisher
American Society for Microbiology
Cited by
25 articles.
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