Molecular Biology and Evolution, Vol 16, 1687-1695, Copyright © 1999 by Society for Molecular Biology and Evolution
MC Enright and BG Spratt
An internal fragment of the ddl gene, encoding the cytoplasmic enzyme D-
alanyl-D-alanine ligase, was sequenced from 566 isolates of Streptococcus
pneumoniae and single isolates of Streptococcus mitis and Streptococcus
oralis. The 52 alleles found among the S. pneumoniae isolates fell into two
groups. Group A alleles were very uniform in sequence and were present in
both penicillin-susceptible and penicillin- resistant pneumococci. Group B
alleles were much more diverse and were found only in penicillin-resistant
isolates. The Streptococcus oralis and Streptococcus mitis alleles were
less diverged from group A alleles than some of the group B pneumococcal
alleles, suggesting that the latter alleles contain interspecies
recombinational replacements. The ddl gene was located 783 bp downstream of
the penicillin-binding protein 2b gene (pbp2b). Sequencing of the
pbp2b-recR-ddl-murF region of three penicillin-resistant pneumococci that
had diverged ddl alleles showed that the whole region from pbp2b to ddl (or
beyond) was highly diverged (about 8%) compared with the sequences from
three penicillin- susceptible isolates. The high levels of diversity in the
group B ddl alleles from penicillin-resistant isolates were ascribed to a
hitchhiking effect whereby interspecies recombinational exchanges at pbp2b,
selected by penicillin usage, often extend into, or through, the ddl gene.
The data allow the average size of the interspecies recombinational
replacements to be estimated at about 6 kb.
ORIGINAL ARTICLE
Extensive variation in the ddl gene of penicillin-resistant Streptococcus pneumoniae results from a hitchhiking effect driven by the penicillin-binding protein 2b gene
Wellcome Trust Centre for the Epidemiology of Infectious Disease, Department of Zoology, University of Oxford, United Kingdom. mark.enright@ceid.ox.ac.uk
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