SpyB, a Small Heme-Binding Protein, Affects the Composition of the Cell Wall in Streptococcus pyogenes
| Autor: | Veronika Tchesnokova, Jing Chen, Lennart S. Forsberg, Haining Zhu, Jeffrey S. Rush, Bernhard Jaehrig, Rebecca J. Edgar, Sashi Kant, Natalia Korotkova, Konstantin V. Korotkov, Parastoo Azadi, Evgeni V. Sokurenko, Vijay Pancholi, Elena Rechkina |
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| Jazyk: | angličtina |
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Hemeproteins Microbiology (medical) Heme binding Streptococcus pyogenes 030106 microbiology Mutant Immunology lcsh:QR1-502 Plasma protein binding Peptidoglycan Biology medicine.disease_cause beta-Lactams Microbiology Bacterial Adhesion lcsh:Microbiology Cell wall 03 medical and health sciences chemistry.chemical_compound Heme-Binding Proteins Drug Resistance Bacterial SpyB medicine SpyA Glycosides N-acetylmuramoyl-L-alanine amidase heme Heme Original Research N-Acetylmuramoyl-L-alanine Amidase 3. Good health Anti-Bacterial Agents Infectious Diseases chemistry Biochemistry Group A carbohydrate cell wall Protein Multimerization ADP-ribosyltransferase Carrier Proteins Gene Deletion Protein Binding |
| Zdroj: | Frontiers in Cellular and Infection Microbiology, Vol 6 (2016) Frontiers in Cellular and Infection Microbiology |
| ISSN: | 2235-2988 |
| DOI: | 10.3389/fcimb.2016.00126 |
| Popis: | Streptococcus pyogenes (Group A Streptococcus or GAS) is a hemolytic human pathogen associated with a wide variety of infections ranging from minor skin and throat infections to life-threatening invasive diseases. The cell wall of GAS consists of peptidoglycan sacculus decorated with a carbohydrate comprising a polyrhamnose backbone with immunodominant N-acetylglucosamine side-chains. All GAS genomes contain the spyBA operon, which encodes a 35-amino-acid membrane protein SpyB, and a membrane-bound C3-like ADP-ribosyltransferase SpyA. In this study, we addressed the function of SpyB in GAS. Phenotypic analysis of a spyB deletion mutant revealed increased bacterial aggregation, and reduced sensitivity to β-lactams of the cephalosporin class and peptidoglycan hydrolase PlyC. Glycosyl composition analysis of cell wall isolated from the spyB mutant suggested an altered carbohydrate structure compared with the wild-type strain. Furthermore, we found that SpyB associates with heme and protoporphyrin IX. Heme binding induces SpyB dimerization, which involves disulfide bond formation between the subunits. Thus, our data suggest the possibility that SpyB activity is regulated by heme. |
| Databáze: | OpenAIRE |
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