scholarly journals The Gene Encoding the Low-Affinity Penicillin-Binding Protein 3r in Enterococcus hirae S185R Is Borne on a Plasmid Carrying Other Antibiotic Resistance Determinants

1998 ◽  
Vol 42 (3) ◽  
pp. 534-539 ◽  
Author(s):  
Dominique Raze ◽  
Olivier Dardenne ◽  
Séverine Hallut ◽  
Manuel Martinez-Bueno ◽  
Jacques Coyette ◽  
...  
Keyword(s):  
Binding Protein ◽  
Bacterial Species ◽  
Multidrug Resistant ◽  
Penicillin Binding Protein ◽  
Enterococcus Hirae ◽  
Erythromycin Resistance ◽  
Gene Encoding ◽  
Transposase Gene ◽  
Encoding Gene ◽  
High Degree

ABSTRACT Two plasmid-derived NcoI DNA fragments of 14 and 4.5 kb, respectively, have been isolated from the multidrug-resistant strain Enterococcus hirae S185R and analyzed. The 14-kb fragment contains two inverted (L and R) IS1216 insertion modules of the ISS1 family. These modules define a Tn5466 transposon-like structure that contains one copy of the methylase-encoding ermAMconferring erythromycin resistance and one copy of the adenylyl-transferase-encoding aadE conferring streptomycin resistance. Immediately on the left side of IS1216L there occurs a copy of pbp3r encoding the low-affinity penicillin-binding protein (PBP) PBP3r, itself preceded by apsr-like gene (psr3r) that controls the synthesis of PBP3r. ermAM, aadE, and the transposase gene (tnp) of IS1216R have the same polarities, and these are opposite those of psr3r,pbp3r, and the tnp gene of IS1216L. The 4.5-kb fragment is a copy of the 4.5-kb sequence at the 5′ end of the 14-kb fragment, although it is not a restriction product of the 14-kb fragment. It contains three genes with the same polarity:psr3r, pbp3r, and tnp in an IS1216 element. Because of the very high degree of identity (99%) with the chromosomal psrfm and pbp5fmgenes of Enterococcus faecium D63R, it is proposed that both the psr3r and pbp3r genes were transferred from an E. faecium strain and inserted in a plasmid ofE. hirae. E. hirae is the first known bacterial species in which a low-affinity PBP-encoding gene has been found to be plasmid borne.

scholarly journals Active-site and membrane topology of the DD-peptidase/penicillin-binding protein no. 6 of Enterococcus hirae (Streptococcus faecium) A.T.C.C. 9790

1989 ◽  
Vol 262 (2) ◽  
pp. 457-462 ◽  
Author(s):  
A el Kharroubi ◽  
G Piras ◽  
P Jacques ◽  
I Szabo ◽  
J Van Beeumen ◽  
...  
Keyword(s):  
Active Site ◽  
Binding Capacity ◽  
Binding Protein ◽  
Membrane Topology ◽  
Penicillin Binding Protein ◽  
Enterococcus Hirae ◽  
Serine Residue ◽  
Membrane Bound ◽  
High Degree ◽  
Terminal Appendage

The membrane-bound 43,000-Mr penicillin-binding protein no. 6 (PBP6) of Enterococcus hirae consists of a 30,000-Mr DD-peptidase/penicillin-binding domain and a approximately 130-residue C-terminal appendage. Removal of this appendage by trypsin proteolysis has no marked effect on the catalytic activity and penicillin-binding capacity of the PBP. Anchorage of the PBP in the membrane appears to be mediated by a short 15-20-residue stretch at the C-terminal end of the appendage. The sequence of the 50-residue N-terminal region of the PBP shows high degree of homology with the sequences of the corresponding regions of the PBPs5 of Escherichia coli and Bacillus subtilis. On this basis the active-site serine residue occurs at position 35 in the enterococcal PBP.

scholarly journals Penicillin-Binding Protein Typing, Antibiotic Resistance Gene Identification, and Molecular Phylogenetic Analysis of Meropenem-Resistant Streptococcus pneumoniae Serotype 19A-CC3111 Strains in Japan

2019 ◽  
Vol 63 (9) ◽  
Author(s):  
Satoshi Nakano ◽  
Takao Fujisawa ◽  
Yutaka Ito ◽  
Bin Chang ◽  
Yasufumi Matsumura ◽  
...  
Keyword(s):  
Multidrug Resistance ◽  
Amino Acid ◽  
Phylogenetic Trees ◽  
Binding Protein ◽  
Antibiotic Resistance Gene ◽  
Multidrug Resistant ◽  
Penicillin Binding Protein ◽  
Motif Analysis ◽  
Molecular Phylogenetic ◽  
Susceptible Clone

ABSTRACT Since the introduction of pneumococcal conjugate vaccines, the prevalence of non-meropenem-susceptible pneumococci has been increasing in Japan. In an earlier study, we demonstrated that multidrug-resistant serotype 15A-ST63 in Japan has a specific pbp1a sequence (pbp1a-13) that could promote meropenem resistance. To trace the origin of pbp1a, we analyzed isolates of serotype 19A-CC3111, which is the most prevalent non-meropenem-susceptible clone in Japan. We analyzed a total of 119 serotype 19A-CC3111 strains recovered in Japan using whole-genome sequencing. Of the 119 isolates, 53 (44.5%) harbored pbp1a-13, indicating that the clone may be the primary reservoir of the pbp1a type and that the pbp1a region may be horizontally transferred between different serotype strains. The single acquisition of pbp1a-13 seemed to cause only penicillin resistance and not multidrug resistance; a combination of penicillin-binding protein (PBP) recombination in the pbp2b and/or pbp2x region(s) with acquisition of pbp1a-13 caused multidrug resistance. Conserved amino acid motif analysis suggested that the pbp1a 370SXXK, pbp2b 448SXN, and pbp2x 337SXXN motifs were the candidates for amino acid substitutions increasing the MICs of meropenem, cefotaxime, and penicillin. We identified a specific clone that was correlated with multidrug resistance, although no correlation was observed between phylogenetic trees generated using core genomes and those generated with only the cps locus. All tested isolates were highly erythromycin resistant, and most harbored mefE within macrolide efflux genetic assembly (MEGA) elements and ermB within Tn917, which was inserted within Tn916 and exhibited a structure identical to that of Tn2017.

scholarly journals Genetic Analyses of Penicillin Binding Protein Determinants in Multidrug-Resistant Streptococcus pneumoniae Serogroup 19 CC320/271 Clone with High-Level Resistance to Third-Generation Cephalosporins

2015 ◽  
Vol 59 (7) ◽  
pp. 4040-4045 ◽  
Author(s):  
Margaret Ip ◽  
Irene Ang ◽  
Veranja Liyanapathirana ◽  
Helen Ma ◽  
Raymond Lai
Keyword(s):  
Hong Kong ◽  
Amino Acid ◽  
Amino Acid Substitution ◽  
Binding Protein ◽  
Multidrug Resistant ◽  
Penicillin Binding Protein ◽  
Unique Amino Acid Substitution ◽  
High Level ◽  
Unique Amino Acid ◽  
Level Resistance

ABSTRACTWe describe the dissemination of a multidrug-resistant (MDR) serogroup 19 pneumococcal clone of representative multilocus sequence type 271 (ST271) with high-level resistance to cefotaxime in Hong Kong and penicillin binding protein (pbp) genes and its relationships to Taiwan19F-14 and the prevalent multidrug-resistant 19A clone (MDR19A-ST320). A total of 472 nonduplicate isolates from 2006 and 2011 were analyzed. Significant increases in the rates of nonsusceptibility to penicillin (PEN) (MIC ≥ 4.0 μg/ml; 9.9 versus 23.3%;P= 0.0005), cefotaxime (CTX) (MIC ≥ 2.0 μg/ml; 12.2 versus 30.3%;P< 0.0001 [meningitis MIC ≥ 1.0 μg/ml; 30.2 versus 48.7%;P= 0.0001]), and erythromycin (ERY) (69.2 versus 84.0%;P= 0.0003) were noted when rates from 2006 and 2011 were compared. The CTX-resistant isolates with MICs of 8 μg/ml in 2011 were of serotype 19F, belonging to ST271. Analyses of the penicillin binding protein 2x (PBP2x) amino acid sequences in relation to the corresponding sequences of the R6 strain revealed M339F, E378A, M400T, and Y595F substitutions found within the ST271 clone but not present in Taiwan19F-14 or MDR19A. In addition, PBP2bs of ST271 strains and that of the Taiwan19F-14 clone were characterized by a unique amino acid substitution, E369D, while ST320 possessed the unique amino acid substitution K366N, as does that of MDR19A in the United States. We hypothesize that ST271 originated from the Taiwan19F-14 lineage, which had disseminated in Hong Kong in the early 2000s, and conferred higher-level β-lactam and cefotaxime resistance through acquisitions of 19 additional amino acid substitutions in PBP2b (amino acid [aa] positions 538 to 641) and altered PBP2x via recombination events. The serogroup 19 MDR CC320/271 clone warrants close monitoring to evaluate its effect after the switch to expanded conjugate vaccines.

Sequence of the penicillin-binding protein 2-encoding gene (penA) of Neisseria perflava/sicca

Gene ◽  
1994 ◽  
Vol 146 (1) ◽  
pp. 91-93 ◽  
Author(s):  
Amalia Perez-Castillo ◽  
Ana M. Perez-Castillo ◽  
Juan A. Saez-Nieto
Keyword(s):  
Binding Protein ◽  
Penicillin Binding Protein ◽  
Encoding Gene ◽  
Neisseria Perflava

scholarly journals Association of Amino Acid Substitutions in Penicillin-Binding Protein 3 with β-Lactam Resistance in β-Lactamase-Negative Ampicillin-Resistant Haemophilus influenzae

2001 ◽  
Vol 45 (6) ◽  
pp. 1693-1699 ◽  
Author(s):  
Kimiko Ubukata ◽  
Yumi Shibasaki ◽  
Kentarou Yamamoto ◽  
Naoko Chiba ◽  
Keiko Hasegawa ◽  
...  
Keyword(s):  
Amino Acid ◽  
Haemophilus Influenzae ◽  
Binding Protein ◽  
Amino Acid Substitutions ◽  
Penicillin Binding Protein ◽  
Gene Encoding ◽  
Group Iii ◽  
Peptidoglycan Synthesis ◽  
Development Of Resistance ◽  
Group I

ABSTRACT The affinity of [3H]benzylpenicillin for penicillin-binding protein (PBP) 3A was reduced in 25 clinical isolates of β-lactamase-negative ampicillin (AMP)-resistant (BLNAR)Haemophilus influenzae for which the AMP MIC was ≥1.0 μg/ml. The affinities of PBP 3B and PBP 4 were also reduced in some strains. The sequences of the ftsI gene encoding the transpeptidase domain of PBP 3A and/or PBP 3B and of thedacB gene encoding PBP 4 were determined for these strains and compared to those of AMP-susceptible Rd strains. The BLNAR strains were classified into three groups on the basis of deduced amino acid substitutions in the ftsI gene, which is thought to be involved in septal peptidoglycan synthesis. His-517, near the conserved Lys-Thr-Gly (KTG) motif, was substituted for Arg-517 in group I strains (n = 9), and Lys-526 was substituted for Asn-526 in group II strains (n = 12). In group III strains (n = 4), three residues (Met-377, Ser-385, and Leu-389), positioned near the conserved Ser-Ser-Asn (SSN) motif, were replaced with Ile, Thr, and Phe, respectively, in addition to the replacement with Lys-526. The MICs of cephem antibiotics with relatively high affinities for PBP 3A and PBP 3B were higher than those of AMP and meropenem for group III strains. The MICs of β-lactams forH. influenzae transformants into which the ftsIgene from BLNAR strains was introduced were as high as those for the donors, and PBP 3A and PBP 3B showed decreased affinities for β-lactams. There was no clear relationship between 7-bp deletions in the dacB gene and AMP susceptibility. Even though mutations in another gene(s) may be involved in β-lactam resistance, these data indicate that mutations in the ftsI gene are the most important for development of resistance to β-lactams in BLNAR strains.

scholarly journals The Enterococcus hirae R40 penicillin-binding protein 5 and the methicillin-resistant Staphylococcus aureus penicillin-binding protein 2′ are similar

1991 ◽  
Vol 280 (2) ◽  
pp. 463-469 ◽  
Author(s):  
A el Kharroubi ◽  
P Jacques ◽  
G Piras ◽  
J Van Beeumen ◽  
J Coyette ◽  
...  
Keyword(s):  
Amino Acid ◽  
Binding Protein ◽  
Water Soluble ◽  
Penicillin Binding Protein ◽  
Enterococcus Hirae ◽  
Methicillin Resistant ◽  
Class B ◽  
Membrane Bound ◽  
Polymerase Chain ◽  
Terminal Domains

The penicillin-resistant Enterococcus hirae R40 has a typical profile of membrane-bound penicillin-binding proteins (PBPs) except that the 71 kDa PBP5 of low penicillin affinity represents about 50% of all the PBPs present. Water-soluble tryptic-digest peptides were selectively produced from PBP5, their N-terminal regions were sequenced and synthetic oligonucleotides were used as primers to generate a 476 bp DNA fragment by polymerase chain reaction. On the basis of these data, the PBP5-encoding gene was cloned in Escherichia coli by using pBR322 as vector. The gene, included in a 7.1 kb insert, had the information for a 678-amino acid-residue protein. PBP5 shows similarity, in the primary structure, with the high-molecular-mass PBPs of class B. In particular, amino acid alignment of the enterococcal PBP5 and the methicillin-resistant staphylococcal PBP2′ generates scores that are 30, for the N-terminal domains, and 53, for the C-terminal domains, standard deviations above that expected for a run of 20 randomized pairs of proteins having the same amino acid compositions as the two proteins under consideration.

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