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Selection of phage-displayed human antibody fragments specific for CD1b presenting the Mycobacterium tuberculosis glycolipid Ac2SGL

Camacho F 1 , Sarmiento ME 2 , Reyes F 1 , Kim L 3 , Huggett J 3 , Lepore M 4 Show all authors , Otero O 5 , Gilleron M 6 , Puzo G 6 , Norazmi MN 7 , Rook G 3 , Mori L 4 , De Libero G 4 , Acosta A 8

Affiliations 

  • 1 Biologicals Sciences School, University of Concepcion, Chile
  • 2 School of Health Sciences, Universiti Sains Malaysia, Malaysia; ADAPT Research Cluster, Centre for Research Initiative, Universiti Sains Malaysia, Malaysia
  • 3 University College London, London, UK
  • 4 Experimental Immunology, University Hospital, Basel, Switzerland
  • 5 Instituto Finlay, Cuba
  • 6 CNRS, Institut de Pharmacologie et de Biologie Structurale, Toulouse, France; Université de Toulouse, UPS, Institut de Pharmacologie et de Biologie Structurale, Toulouse, France
  • 7 School of Health Sciences, Universiti Sains Malaysia, Malaysia; ADAPT Research Cluster, Centre for Research Initiative, Universiti Sains Malaysia, Malaysia; Institute for Research in Molecular Medicine, Universiti Sains Malaysia, Malaysia
  • 8 ADAPT Research Cluster, Centre for Research Initiative, Universiti Sains Malaysia, Malaysia; Institute for Research in Molecular Medicine, Universiti Sains Malaysia, Malaysia. Electronic address: aracosta2001@yahoo.com
Int J Mycobacteriol, 2016 06;5(2):120-7.
PMID: 27242221 DOI: 10.1016/j.ijmyco.2015.12.002

Abstract

OBJECTIVE/BACKGROUND: The development of new tools capable of targeting Mycobacterium tuberculosis (Mtb)-infected cells have potential applications in diagnosis, treatment, and prevention of tuberculosis. In Mtb-infected cells, CD1b molecules present Mtb lipids to the immune system (Mtb lipid-CD1b complexes). Because of the lack of CD1b polymorphism, specific Mtb lipid-CD1b complexes could be considered as universal Mtb infection markers. 2-Stearoyl-3-hydroxyphthioceranoyl-2'-sulfate-α-α'-d-trehalose (Ac2SGL) is specific for Mtb, and is not present in other mycobacterial species. The CD1b-Ac2SGL complexes are expressed on the surface of human cells infected with Mtb. The aim of this study was to generate ligands capable of binding these CD1b-Ac2SGL complexes.

METHODS: A synthetic human scFv phage antibody library was used to select phage-displayed antibody fragments that recognized CD1b-Ac2SGL using CD1b-transfected THP-1 cells loaded with Ac2SGL.

RESULTS: One clone, D11-a single, light-variable domain (kappa) antibody (dAbκ11)-showed high relative binding to the Ac2SGL-CD1b complex.

CONCLUSION: A ligand recognizing the Ac2SGL-CD1b complex was obtained, which is a potential candidate to be further tested for diagnostic and therapeutic applications.

* Title and MeSH Headings from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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