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PMID: 2543637 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Conservation of the biologically active portions of staphylococcal enterotoxins C1 and C2.

Infection and immunity ·Vol. 57 ·No. 7 ·1989-07-00 ·Pages 2249-52

Bohach GA, Schlievert PM

Abstract

We determined the primary sequence of staphylococcal enterotoxin (SE) C2 by sequencing its cloned structural gene, entC2. The entC2 structural gene contains an 801-base-pair open reading frame which encodes a 266-amino-acid precursor with a molecular weight of 30,608. Mature SE C2, produced by removal of the signal peptide, contains 239 amino acids with a molecular weight of 27,531. A sequence comparison between SE C2 and SE C1 showed that the 167 carboxyl amino acids in both toxins were 100% conserved. In contrast, the 72 N-terminal residues were 10% divergent. This provides additional evidence that carboxyl regions of staphylococcal and streptococcal pyrogenic toxins determine shared biological activities and cross-reactive epitopes.

MeSH Terms
Amino Acid Sequence Antigens, Bacterial/genetics,isolation & purification Bacterial Proteins/genetics,isolation & purification,toxicity Base Sequence Enterotoxins/genetics,isolation & purification,toxicity Genes, Bacterial Molecular Sequence Data Sequence Homology, Nucleic Acid Staphylococcus aureus/genetics,physiology
Chemicals
Antigens, Bacterial Bacterial Proteins Enterotoxins enterotoxin C, staphylococcal
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Bohach G A
Department of Microbiology, Medical School, University of Minnesota, Minneapolis 55455.
Schlievert P M
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Article Info
Journal
Infection and immunity
Abbr.
Infect Immun
ISSN
0019-9567
Published
1989-07-00
Pages
2249-52
Language
English
Region
United States
NLM ID
0246127
PMCID
PMC313868
Subset
IM
Grants
NHLBI NIH HHS · HL36611 · United States
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