Navegando por Palavras-chave "metallo-beta-lactamase"

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    Carbapenem-resistant Pseudomonas aeruginosa - clonal spread in Southern Brazil and in the State of Goias
    (Contexto, 2010-09-01) Scheffer, Mara Cristina; Gales, Ana Cristina [UNIFESP]; Barth, Afonso Luis; Carmo Filho, Jose Rodrigues do; Dalla-Costa, Libera Maria; Univ Fed Parana; Universidade Federal de Santa Catarina (UFSC); Universidade Federal de São Paulo (UNIFESP); Hosp Clin Porto Alegre; Univ Catolica Goias; Fac Pequeno Principe
    This study evaluated the clonal spread of carbapenem-resistant P. aeruginosa producing SPM-1 type metallo-beta-lactamase (MBL), at the university hospital of Florianopolis, Santa Catarina, Brazil, compared to an epidemic clone previously reported, as well as strains collected in other three Brazilian states. Among the isolates, 17 (62%) were clonal and highly related to strains from other regions of Brazil. Six clonal strains harbored the bla(SPM-1) gene. the finding of a unique SPM-1 producer clone suggests that its dissemination has contributed to the high resistance to carbapenems in Brazilian hospitals.
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    Molecular characterization of SPM-1, a novel metallo-beta-lactamase isolated in Latin America: report from the SENTRY antimicrobial surveillance programme
    (Oxford Univ Press, 2002-11-01) Toleman, M. A.; Simm, A. M.; Murphy, T. A.; Gales, Ana C. [UNIFESP]; Biedenbach, D. J.; Jones, R. N.; Walsh, T. R.; Univ Bristol; Universidade Federal de São Paulo (UNIFESP); JONES Grp JMI Labs; Tufts Univ
    The gene encoding the metallo-beta-lactamase SPM-1 was cloned from a genomic library of Pseudomonas aeruginosa strain 48-1997A. the insert carrying spm-1 possessed a GC content of 47%, indicating that it is of non-Pseudomonas origin. Upstream of spm-1 there is a small open reading frame (ORF), which is homologous to the LysR family of proteins (69% identity to the LysR protein from Salmonella enterica serovar Typhimurium). Downstream of spm-1 there is the start of an ORF, the product of which shows close homology with the GroEL-type proteins from Xanthomonas campestris. No transmissible element could be identified upstream or downstream of spm-1. the spm-1 gene is carried on a plasmid that can transform both Escherichia coli and P. aeruginosa to ceftazidime resistance. SPM-1 contains the classic metallo-beta-lactamase zinc-binding motif HXHXD and shows the highest identity (35.5%) to IMP-1. SPM-1 is a distinctly different metallo-beta-lactamase from VIM and IMP and, accordingly, represents a new subfamily of mobile metallo-beta-lactamases. the predicted molecular weight of the protein was 27515 Da, significantly higher than that of IMP (25041 Da) or VIM (25322 Da). SPM-1 possesses a unique loop of 23 residues that accounts for the higher molecular mass.
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    Occurrence of IMP-1 in non-baumannii Acinetobacter clinical isolates from Brazil
    (Microbiology Soc, 2018) Cayô, Rodrigo [UNIFESP]; Streling, Ana Paula [UNIFESP]; Nodari, Carolina Silva [UNIFESP]; Matos, Adriana Pereira [UNIFESP]; Luz, Adryella de Paula [UNIFESP]; Dijkshoorn, Lenie; Pignatari, Antonio Carlos Campos [UNIFESP]; Gales, Ana Cristina [UNIFESP]
    The aim of this study was to characterize the presence of carbapenemase-encoding genes in distinct species of Acinetobacter spp. isolated from Brazilian hospitals. Five carbapenem-resistant Acinetobacter spp. isolates (two Acinetobacter pittii, two Acinetobacter bereziniae and one Acinetobacter junii) recovered from two distinct hospitals between 2000 and 2016 were included in this study. All of the isolates harboured bla(IMP-1), which was inserted into In86, a class 1 integron. Pulsed field gel eletrophoresis analysis showed that both A. pittii were identical, while the two A. berezinae isolates were considered to be clonally related. In this study, we demonstrated that mobile elements carrying carbapenemase-encoding genes such as In86 may persist for a long period, allowing their mobilization from A. baumannii to other Acinetobacter spp. that are usually susceptible to multiple antimicrobials.