Development of Nanobodies as Theranostic Agents against CMY-2-Like Class C β-Lactamases-Reference-Cited by-同舟云学术

Development of Nanobodies as Theranostic Agents against CMY-2-Like Class C β-Lactamases

Published:2023-04-18 Issue:4 Volume:67 Page:
ISSN:0066-4804
Container-title:Antimicrobial Agents and Chemotherapy
language:en
Short-container-title:Antimicrob Agents Chemother

Author:

Cawez Frédéric¹,Mercuri Paola Sandra¹,Morales-Yãnez Francisco Javier²³,Maalouf Rita²,Vandevenne Marylène⁴,Kerff Frederic⁵,Guérin Virginie⁶,Mainil Jacques⁶^ORCID,Thiry Damien⁶^ORCID,Saulmont Marc⁷,Vanderplasschen Alain³⁸,Lafaye Pierre⁹,Aymé Gabriel⁹,Bogaerts Pierre¹⁰^ORCID,Dumoulin Mireille²³,Galleni Moreno¹^ORCID

Affiliation:

1. InBioS, Center for Protein Engineering, Biological Macromolecules, Department of Life Sciences, University of Liège, Liège, Belgium

2. InBioS, Center for Protein Engineering, NEPTUNS, Department of Life Sciences, University of Liège, Liège, Belgium

3. ALPANANO, Center for Protein Engineering & FARAH, University of Liège, Liège, Belgium

4. InBios, Center for Protein Engineering, ROBOTEIN, Department of Life Sciences, University of Liège, Liège, Belgium

5. InBioS, Center for Protein Engineering, Department of Life Sciences, University of Liège, Liège, Belgium

6. Bacteriology, FARAH and Faculty of Veterinary Medicine, Department of Infectious and Parasitic Diseases, University of Liège, Liège, Belgium

7. Regional Animal Health and Identification Association (ARSIA), Ciney, Belgium

8. Immunology-Vaccinology, FARAH and Faculty of Veterinary Medicine, Department of Infectious and Parasitic Diseases, University of Liège, Liège, Belgium

9. Institut Pasteur, Université Paris Cité, CNRS UMR 328, Paris, France

10. National Reference Center for Antibiotic-Resistant Gram-Negative Bacilli, Department of Clinical Microbiology, CHU UCL Namur, Yvoir, Belgium

Abstract

Three soluble single-domain fragments derived from the unique variable region of camelid heavy-chain antibodies (VHHs) against the CMY-2 β-lactamase behaved as inhibitors. The structure of the complex VHH cAb CMY-2 (254)/CMY-2 showed that the epitope is close to the active site and that the CDR3 of the VHH protrudes into the catalytic site.

Funder

Federal Public Service Health, Food Chain safety and Environment

Fonds De La Recherche Scientifique - FNRS

Universite de liege

Publisher

American Society for Microbiology

Subject

Infectious Diseases,Pharmacology (medical),Pharmacology

Link

https://journals.asm.org/doi/pdf/10.1128/aac.01499-22

Reference52 articles.

1. O’Neill J. 2016. Tackling drug-resistant infections globally: report and recommendations. Wellcome Trust and UK Government, London, United Kingdom. https://amr-review.org/.

2. β-Lactams and β-Lactamase Inhibitors: An Overview

3. Bacterial Resistance to β-Lactam Antibiotics: Compelling Opportunism, Compelling Opportunity

4. Mechanism of action of penicillins: a proposal based on their structural similarity to acyl-D-alanyl-D-alanine.

5. Structural basis for the β lactam resistance of PBP2a from methicillin-resistant Staphylococcus aureus

Cited by 2 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Mono- and Bi-specific Nanobodies Targeting the CUB Domains of PCPE-1 Reduce the Proteolytic Processing of Fibrillar Procollagens;Journal of Molecular Biology;2024-08

2. Broadly Reactive Nanobody Targeting the H3 Hemagglutinin of the Influenza A Virus;Acta Naturae;2024-05-10