Bibliographic Details
| Title: |
Relationship between Penicillin-Binding Proteins Alterations and β-Lactams Non-Susceptibility of Diseased Pig-Isolated Streptococcus suis |
| Authors: |
Kamonwan Lunha, Wiyada Chumpol, Surasak Jiemsup, Sukuma Samngamnim, Pornchalit Assavacheep, Suganya Yongkiettrakul |
| Source: |
Antibiotics, Vol 12, Iss 1, p 158 (2023) |
| Publisher Information: |
MDPI AG, 2023. |
| Publication Year: |
2023 |
| Collection: |
LCC:Therapeutics. Pharmacology |
| Subject Terms: |
β-lactams resistance, penicillin resistance, penicillin-binding proteins, Streptococcus suis, Therapeutics. Pharmacology, RM1-950 |
| More Details: |
Streptococcus suis is a zoonotic pathogen causing disease in both animals and humans, and the emergence of increasingly resistant bacteria to antimicrobial agents has become a significant challenge globally. The objective of this study was to investigate the genetic basis for declining susceptibility to penicillin and other β-lactams among S. suis. Antimicrobial susceptibility testing and penicillin-binding proteins (PBP1a, PBP2a, PBP2b, and PBP2x) sequence analysis were performed on 225 S. suis isolated from diseased pigs. This study found that a growing trend of isolates displayed reduced susceptibility to β-lactams including penicillin, ampicillin, amoxicillin/clavulanic acid, and cephalosporins. A total of 342 substitutions within the transpeptidase domain of four PBPs were identified, of which 18 substitutions were most statistically associated with reduced β-lactams susceptibility. Almost all the S. suis isolates which exhibited penicillin-non-susceptible phenotype (71.9%) had single nucleotide polymorphisms, leading to alterations of PBP1a (P409T) and PBP2a (T584A and H588Y). The isolates may manifest a higher level of penicillin resistance by additional mutation of M341I in the 339STMK active site motif of PBP2x. The ampicillin-non-susceptible isolates shared the mutations in PBP1a (P409T) and PBP2a (T584A and H588Y) with additional alterations of PBP2b (T625R) and PBP2x (T467S). The substitutions, including PBP1a (M587S/T), PBP2a (M433T), PBP2b (I428L), and PBP2x (Q405E/K/L), appeared to play significant roles in mediating the reduction in amoxicillin/clavulanic acid susceptibility. Among the cephalosporins, specific mutations strongly associated with the decrease in cephalosporins susceptibility were observed for ceftiofur: PBP1a (S477D/G), PBP2a (E549Q and A568S), PBP2b (T625R), and PBP2x (Q453H). It is concluded that there was genetically widespread presence of PBPs substitutions associated with reduced susceptibility to β-lactam antibiotics. |
| Document Type: |
article |
| File Description: |
electronic resource |
| Language: |
English |
| ISSN: |
2079-6382 |
| Relation: |
https://www.mdpi.com/2079-6382/12/1/158; https://doaj.org/toc/2079-6382 |
| DOI: |
10.3390/antibiotics12010158 |
| Access URL: |
https://doaj.org/article/5e47e3a6e1da4c8b87c3d1de4b21dccf |
| Accession Number: |
edsdoj.5e47e3a6e1da4c8b87c3d1de4b21dccf |
| Database: |
Directory of Open Access Journals |
