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Infection and Immunity, March 2001, p. 1729-1738, Vol. 69, No. 3
Department of Pathology, Baylor College of
Medicine, Houston, Texas 77030,1 and
Laboratory of Human Bacterial Pathogenesis, Rocky Mountain
Laboratories, National Institute of Allergy and Infectious
Diseases, National Institutes of Health, Hamilton, Montana
598402
Received 31 October 2000/Returned for modification 27 November
2000/Accepted 29 November 2000
A recent study found that group A Streptococcus (GAS)
expresses a cell surface protein with similarity to human collagen (S. Lukomski, K. Nakashima, I. Abdi, V. J. Cipriano, R. M. Ireland, S. R. Reid, G. G. Adams, and J. M. Musser,
Infect. Immun. 68:6542-6553, 2000). This streptococcal collagen-like
protein (Scl) contains a long region of Gly-X-X motifs and was produced
by serotype M1 GAS strains. In the present study, a second member of
the scl gene family was identified and designated
scl2. The Scl2 protein also has a collagen-like region,
which in M1 strains is composed of 38 contiguous Gly-X-X triplet
motifs. The scl2 gene was present in all 50 genetically
diverse GAS strains studied. The Scl2 protein is highly polymorphic,
and the number of Gly-X-X motifs in the 50 strains studied ranged from
31 in one serotype M1 strain to 79 in serotype M28 and M77 isolates.
The scl1 and scl2 genes were simultaneously
transcribed in the exponential phase, and the Scl proteins were also
produced. Scl1 and Scl2 were identified in a cell-associated form and
free in culture supernatants. Production of Scl1 is regulated
by Mga, a positive transcriptional regulator that controls expression
of several GAS virulence factors. In contrast, production of Scl2 is
controlled at the level of translation by variation in the number of
short-sequence pentanucleotide repeats (CAAAA) located immediately
downstream of the GTG (Val) start codon. Control of protein production
by this molecular mechanism has not been identified previously in GAS.
Together, the data indicate that GAS simultaneously produces two
extracellular human collagen-like proteins in a regulated fashion.
0019-9567/01/$04.00+0 DOI: 10.1128/IAI.69.3.1729-1738.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
Identification and Characterization of a Second
Extracellular Collagen-Like Protein Made by Group A
Streptococcus: Control of Production at the Level
of Translation

*
Corresponding author. Mailing address: Laboratory of
Human Bacterial Pathogenesis, Rocky Mountain Laboratories, National
Institute of Allergy and Infectious Diseases, National Institutes of
Health, 903 South 4th St., Hamilton, MT 59840. Phone: (406) 363-9315. Fax: (406) 363-9427. E-mail: jmusser{at}niaid.nih.gov.
Present address: Department of Respiratory Diseases, Chubu National
Hospital, Aichi 474-8511, Japan.
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