PBP2a in β-Lactam-Resistant Laboratory Mutants and Clinical Isolates: Disruption Versus Reduced Penicillin Affinity.
PBP2a in β-Lactam-Resistant Laboratory Mutants and Clinical Isolates: Disruption Versus Reduced Penicillin Affinity.
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β-内酰胺抗性实验室突变体和临床分离株中的 PBP2a:破坏与青霉素亲和力降低
DOI:
10.1089/mdr.2017.0302
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发表时间:
2017
影响因子:
2.6
通讯作者:
Regine
中科院分区:
文献类型:
--
作者:
van der Linden;Rutschmann;Maurer;Patrick;Hakenbeck;Regine
Alterations in PBP2a have been recognized in cefotaxime-resistant laboratory mutants and β-lactam–resistant clinical isolates ofStreptococcus pneumoniae. DNA sequencing revealed fundamental differences between these two settings. Internal stop codons inpbp2aoccurred in all three laboratory mutants analyzed, caused by a mutation inpbp2aof mutant C604, and tandem duplications withinpbp2aresulting in premature stop codons in another two mutants C403 and C406. In contrast, mosaic PBP2a genes were observed in several penicillin-resistant clinical isolates from South Africa, the Czech Republic, Hungary, and in the clone Poland23F-16, with sequence blocks diverging from sensitive strains by over 4%. Most of thesepbp2avariants exceptpbp2afrom the South African strain contained sequences related topbp2aofStreptococcus mitisB6, confirming that this species serves as reservoir for penicillin-resistance determinants.
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影响因子:
2.6
作者:
M. du Plessis;A. M. Smith;K. Klugman
通讯作者:
M. du Plessis;A. M. Smith;K. Klugman
影响因子:
3.6
作者:
Geneviève Alioing;Chantal Granadel;D. Morrison;J. Claverys
通讯作者:
J. Claverys
影响因子:
3.6
作者:
C. Sibold;J. Henrichsen;A. König;Christian Martín;L. Chalkley;R. Hakenbeck
通讯作者:
R. Hakenbeck
影响因子:
3.1
作者:
KISLAK, JW;RAZAVI, LMB;FINLAND, M
通讯作者:
FINLAND, M
影响因子:
5.2
作者:
Fani, Fereshteh;Brotherton, Marie-Christine;Ouellette, Marc
通讯作者:
Ouellette, Marc