Degradation of penicillin-binding protein 2' in methicillin-resistant staphylococcus aureus

Y. Sumita; M. Fukasawa; S. Mitsuhashi; M. Inoue

doi:10.1159/000239340

Degradation of penicillin-binding protein 2' in methicillin-resistant staphylococcus aureus

Y. Sumita, M. Fukasawa, S. Mitsuhashi, M. Inoue

University Hospital

Research output: Contribution to journal › Article › peer-review

1 Citation (Scopus)

Abstract

We detected a novel protein with [¹⁴C]benzylpenicillin (PCG)- binding capacity and a molecular mass of about 60 kD in meth- icillin-resistant Staphylococcus aureus using a high concentration of [¹⁴C]PCG and extending the reaction time. However, the fluorogram showed that the band density of penicillin- binding protein 2' (PBP2') decreased gradually with incubation time. The appearance of the 60-kD protein and the reduction of the band density of PBP2' were stoichiometrically linked, and the binding profiles of p-lactams for PBP2' and the 60-kD protein corresponded. These results suggested that the 60-kD protein is a degradation product of PBP2.

Original language	English
Pages (from-to)	172-177
Number of pages	6
Journal	CHEMOTHERAPY
Volume	41
Issue number	3
DOIs	https://doi.org/10.1159/000239340
Publication status	Published - Jan 1 1995

Keywords

Degradation
Mcthicillin-resistant
P-Lactams
Penicillin-binding protein 2
Staphylococcus aureus

ASJC Scopus subject areas

Oncology
Pharmacology
Drug Discovery
Pharmacology (medical)
Infectious Diseases

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1159/000239340

Cite this

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title = "Degradation of penicillin-binding protein 2' in methicillin-resistant staphylococcus aureus",

abstract = "We detected a novel protein with [14C]benzylpenicillin (PCG)- binding capacity and a molecular mass of about 60 kD in meth- icillin-resistant Staphylococcus aureus using a high concentration of [14C]PCG and extending the reaction time. However, the fluorogram showed that the band density of penicillin- binding protein 2' (PBP2') decreased gradually with incubation time. The appearance of the 60-kD protein and the reduction of the band density of PBP2' were stoichiometrically linked, and the binding profiles of p-lactams for PBP2' and the 60-kD protein corresponded. These results suggested that the 60-kD protein is a degradation product of PBP2.",

keywords = "Degradation, Mcthicillin-resistant, P-Lactams, Penicillin-binding protein 2, Staphylococcus aureus",

author = "Y. Sumita and M. Fukasawa and S. Mitsuhashi and M. Inoue",

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T1 - Degradation of penicillin-binding protein 2' in methicillin-resistant staphylococcus aureus

AU - Sumita, Y.

AU - Fukasawa, M.

AU - Mitsuhashi, S.

AU - Inoue, M.

PY - 1995/1/1

Y1 - 1995/1/1

N2 - We detected a novel protein with [14C]benzylpenicillin (PCG)- binding capacity and a molecular mass of about 60 kD in meth- icillin-resistant Staphylococcus aureus using a high concentration of [14C]PCG and extending the reaction time. However, the fluorogram showed that the band density of penicillin- binding protein 2' (PBP2') decreased gradually with incubation time. The appearance of the 60-kD protein and the reduction of the band density of PBP2' were stoichiometrically linked, and the binding profiles of p-lactams for PBP2' and the 60-kD protein corresponded. These results suggested that the 60-kD protein is a degradation product of PBP2.

AB - We detected a novel protein with [14C]benzylpenicillin (PCG)- binding capacity and a molecular mass of about 60 kD in meth- icillin-resistant Staphylococcus aureus using a high concentration of [14C]PCG and extending the reaction time. However, the fluorogram showed that the band density of penicillin- binding protein 2' (PBP2') decreased gradually with incubation time. The appearance of the 60-kD protein and the reduction of the band density of PBP2' were stoichiometrically linked, and the binding profiles of p-lactams for PBP2' and the 60-kD protein corresponded. These results suggested that the 60-kD protein is a degradation product of PBP2.

KW - Degradation

KW - Mcthicillin-resistant

KW - P-Lactams

KW - Penicillin-binding protein 2

KW - Staphylococcus aureus

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Degradation of penicillin-binding protein 2' in methicillin-resistant staphylococcus aureus

Abstract

Keywords

ASJC Scopus subject areas

UN SDGs

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