Structural basis for antibiotic resistance by chloramphenicol acetyltransferase type A in Staphylococcus aureus
文献类型：期刊论文
| 作者 | Wang, Kaiyue2,3; Chen, Junwei2,3; Li, Wanfang4; Wang, Min5; Fan, Tingwen6; Bu, Dongbo1,7; Ye, Sheng2,3,8 |
| 刊名 | SCIENTIFIC REPORTS
 |
| 出版日期 | 2025-10-23 |
| 卷号 | 15期号:1页码:13 |
| 关键词 | |
| ISSN号 | 2045-2322 |
| DOI | 10.1038/s41598-025-18365-4 |
| 英文摘要 | Methicillin-resistant Staphylococcus aureus (MRSA) exemplifies high-level antibiotic resistance in this major human pathogen. Its resistance to chloramphenicol is majorly conferred by enzymatic inactivation via chloramphenicol acetyltransferases (CATs). This modification sterically blocks the antibiotic's ribosomal binding and thus neutralizes its inhibitory potency. Although CATs have been structurally studied across diverse bacteria species, the structures of S. aureus CATs (saCATs) have remained uncharacterized. To address this gap and elucidate species-specific resistance mechanisms, we determined the first high-resolution crystal structure of saCAT1, the prototypical saCAT enzyme. Structural analysis delineates the active site architecture and reveals the molecular basis for substrate recognition of both chloramphenicol and fusidic acid (FA). Further enzymatic assays demonstrated that the Km value against chloramphenicol is 16.9 mu M, and the Ki value of the inhibitor FA is 83.7 mu M, indicating that the inhibitory capacity of FA is relatively limited. These findings provide an essential structural framework for understanding chloramphenicol resistance in S. aureus and facilitate the rational design of novel antimicrobial strategies to combat multidrug-resistant pathogens. |
| 资助项目 | Beijing Municipal Science & Technology Commission grant ; Beijing Regional Center of Large Research Instruments for Life Sciences |
| WOS研究方向 | Science & Technology - Other Topics |
| 语种 | 英语 |
| WOS记录号 | WOS:001600537100011 |
| 出版者 | NATURE PORTFOLIO |
| 源URL | [http://119.78.100.204/handle/2XEOYT63/41590]  |
| 专题 | 中国科学院计算技术研究所期刊论文_英文 |
| 通讯作者 | Bu, Dongbo; Ye, Sheng |
| 作者单位 | 1.Univ Chinese Acad Sci, Beijing 100080, Peoples R China 2.Beihang Univ, Sch Biomed Sci & Med Engn, Beijing 100191, Peoples R China 3.Beihang Univ, Key Lab Big Data Based Precis Med, Minist Ind & Informat Technol, Beijing 100862, Peoples R China 4.Rutgers State Univ, Sch Arts & Sci, New Brunswick, NJ 08901 USA 5.Chinese Acad Sci, Inst Biophys, State Key Lab Biomacromol, Beijing 100101, Peoples R China 6.Chinese Acad Sci, Inst Microbiol, State Key Lab Microbial Divers & Innovat Utilizat, Beijing 100101, Peoples R China 7.Chinese Acad Sci, SKLP, Inst Comp Technol, Beijing 100190, Peoples R China 8.Beihang Univ, Sch Engn Med, Beijing 100191, Peoples R China |
| 推荐引用方式 GB/T 7714 | Wang, Kaiyue,Chen, Junwei,Li, Wanfang,et al. Structural basis for antibiotic resistance by chloramphenicol acetyltransferase type A in Staphylococcus aureus[J]. SCIENTIFIC REPORTS,2025,15(1):13. |
| APA | Wang, Kaiyue.,Chen, Junwei.,Li, Wanfang.,Wang, Min.,Fan, Tingwen.,...&Ye, Sheng.(2025).Structural basis for antibiotic resistance by chloramphenicol acetyltransferase type A in Staphylococcus aureus.SCIENTIFIC REPORTS,15(1),13. |
| MLA | Wang, Kaiyue,et al."Structural basis for antibiotic resistance by chloramphenicol acetyltransferase type A in Staphylococcus aureus".SCIENTIFIC REPORTS 15.1(2025):13. |
入库方式： OAI收割
来源：计算技术研究所
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