Journal article
Conservation of the biologically active portions of staphylococcal enterotoxins C1 and C2
Infection and immunity, Vol.57(7), pp.2249-2252
07/1989
DOI: 10.1128/IAI.57.7.2249-2252.1989
PMCID: PMC313868
PMID: 2543637
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.
Details
- Title: Subtitle
- Conservation of the biologically active portions of staphylococcal enterotoxins C1 and C2
- Creators
- Gregory A Bohach - Department of Microbiology, Medical School, University of Minnesota, Minneapolis 55455Patrick M Schlievert
- Resource Type
- Journal article
- Publication Details
- Infection and immunity, Vol.57(7), pp.2249-2252
- Publisher
- United States
- DOI
- 10.1128/IAI.57.7.2249-2252.1989
- PMID
- 2543637
- PMCID
- PMC313868
- ISSN
- 0019-9567
- eISSN
- 1098-5522
- Grant note
- HL36611 / NHLBI NIH HHS
- Language
- English
- Date published
- 07/1989
- Academic Unit
- Microbiology and Immunology; Internal Medicine
- Record Identifier
- 9984001154902771
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