TY - JOUR
T1 - New CTX‐M group conferring β‐lactam resistance
T2 - a compendium of phylogenetic insights from biochemical, molecular, and structural biology
AU - Mendonça, Jacinta
AU - Guedes, Carla
AU - Silva, Carina
AU - Sá, Sara
AU - Oliveira, Marco
AU - Accioly, Gustavo
AU - Baylina, Pilar
AU - Barata, Pedro
AU - Pereira, Cláudia
AU - Fernandes, Ruben
N1 - Funding Information:
Funding: This research received with the support of the “Programa Operacional Regional do Norte” (Norte2020), by Portugal 2020 and the “Fundo Europeu de Desenvolvimento Regional” (FEDER) (Norte‐01‐0145‐FEDER‐000012), by Fundação para Ciência e Tecnologia FCT) UID/BIM/04293/2013 and cofunded by the projects FEDER/02/SAICT/2020/072560, RESEARCH4COVID, 104_596694627, RESEARCH4COVID 112_596698921, AND RESEARCH4COVID 2nd ED 418_613508517.
Publisher Copyright:
© 2022 by the authors. Licensee MDPI, Basel, Switzerland.
PY - 2022/2
Y1 - 2022/2
N2 - The production of extended‐spectrum β‐lactamases (ESBLs) is the main defense mechanism found in Gram negative bacteria. Among all the ESBLs, the CTX‐M enzymes appear as the most efficient in terms of dissemination in different epidemiological contexts. CTX‐M enzymes exhibit a striking plas-ticity, with a large number of allelic variants distributed in several sublineages, which can be associated with functional heterogeneity of clinical relevance. This observational analytical study provides an update of this family, currently with more than 200 variants described, from a phylogenetic, molecular, and structural point of view through homology in amino acid sequences. Our data, combined with described literature, provide phylogenetic and structural evidence of a new group. Thus, herein, we propose six groups among CTX‐M enzymes: the already stablished CTX‐M‐1, CTX‐M‐2, CTX‐M‐8, CTX‐M‐9, and CTX‐M‐25 clusters, as well as CTX‐M‐151 as the new cluster.
AB - The production of extended‐spectrum β‐lactamases (ESBLs) is the main defense mechanism found in Gram negative bacteria. Among all the ESBLs, the CTX‐M enzymes appear as the most efficient in terms of dissemination in different epidemiological contexts. CTX‐M enzymes exhibit a striking plas-ticity, with a large number of allelic variants distributed in several sublineages, which can be associated with functional heterogeneity of clinical relevance. This observational analytical study provides an update of this family, currently with more than 200 variants described, from a phylogenetic, molecular, and structural point of view through homology in amino acid sequences. Our data, combined with described literature, provide phylogenetic and structural evidence of a new group. Thus, herein, we propose six groups among CTX‐M enzymes: the already stablished CTX‐M‐1, CTX‐M‐2, CTX‐M‐8, CTX‐M‐9, and CTX‐M‐25 clusters, as well as CTX‐M‐151 as the new cluster.
KW - CTX‐M β‐lactamases
KW - CTX‐M‐151 new group
KW - Extended‐spectrum β‐lactamases (ESBL)
UR - http://www.scopus.com/inward/record.url?scp=85124403836&partnerID=8YFLogxK
U2 - 10.3390/biology11020256
DO - 10.3390/biology11020256
M3 - Article
C2 - 35205122
AN - SCOPUS:85124403836
SN - 2079-7737
VL - 11
JO - Biology
JF - Biology
IS - 2
M1 - 256
ER -