Isolation and preliminary characterization of a human 'phage display'-derived antibody against neural adhesion molecule-1 antigen interfering with fibroblast growth factor receptor-1 binding.


Journal

Human antibodies
ISSN: 1875-869X
Titre abrégé: Hum Antibodies
Pays: Netherlands
ID NLM: 9711270

Informations de publication

Date de publication:
2021
Historique:
pubmed: 10 11 2020
medline: 10 9 2021
entrez: 9 11 2020
Statut: ppublish

Résumé

The NCAM or CD56 antigen is a cell surface glycoprotein belonging to the immunoglobulin super-family involved in cell-cell and cell-matrix adhesion. NCAM is also over-expressed in many tumour types and is considered a tumour associated antigen, even if its role and biological mechanisms implicated in tumour progression and metastasis have not yet to be elucidated. In particular, it is quite well documented the role of the interaction between the NCAM protein and the fibroblast growth factor receptor-1 in metastasis and invasion, especially in the ovarian cancer progression. Here we describe the isolation and preliminary characterization of a novel human anti-NCAM single chain Fragment variable antibody able to specifically bind NCAM-expressing cells, including epithelial ovarian cancer cells. The antibody was isolate by phage display selection and was characterized by ELISA, FACS analysis and SPR experiments. Interference in EOC migration was analyzed by scratch test. It binds a partially linear epitope lying in the membrane proximal region of two fibronectin-like domains with a dissociation constant of 3.43 × 10-8 M. Interestingly, it was shown to interfere with the NCAM-FGFR1 binding and to partially decrease migration of EOC cells. According to our knowledge, this is the first completely human antibody able to interfere with this newly individuated cancer mechanism.

Sections du résumé

BACKGROUND BACKGROUND
The NCAM or CD56 antigen is a cell surface glycoprotein belonging to the immunoglobulin super-family involved in cell-cell and cell-matrix adhesion. NCAM is also over-expressed in many tumour types and is considered a tumour associated antigen, even if its role and biological mechanisms implicated in tumour progression and metastasis have not yet to be elucidated. In particular, it is quite well documented the role of the interaction between the NCAM protein and the fibroblast growth factor receptor-1 in metastasis and invasion, especially in the ovarian cancer progression.
OBJECTIVE OBJECTIVE
Here we describe the isolation and preliminary characterization of a novel human anti-NCAM single chain Fragment variable antibody able to specifically bind NCAM-expressing cells, including epithelial ovarian cancer cells.
METHODS METHODS
The antibody was isolate by phage display selection and was characterized by ELISA, FACS analysis and SPR experiments. Interference in EOC migration was analyzed by scratch test.
RESULTS RESULTS
It binds a partially linear epitope lying in the membrane proximal region of two fibronectin-like domains with a dissociation constant of 3.43 × 10-8 M. Interestingly, it was shown to interfere with the NCAM-FGFR1 binding and to partially decrease migration of EOC cells.
CONCLUSIONS CONCLUSIONS
According to our knowledge, this is the first completely human antibody able to interfere with this newly individuated cancer mechanism.

Identifiants

pubmed: 33164927
pii: HAB200431
doi: 10.3233/HAB-200431
doi:

Substances chimiques

Immunoglobulins 0
Neural Cell Adhesion Molecules 0

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

63-84

Auteurs

Michela Flego (M)

National Center for Global Health, Istituto Superiore di Sanità, Rome, Italy.

Gianni Colotti (G)

Institute of Molecular Biology and Pathology, Italian National Research Council, c/o Department Biochemical Sciences, Sapienza University of Rome, Rome, Italy.

Alessandro Ascione (A)

National Center for Control and Evaluation of Medicine, Istituto Superiore di Sanità, Rome, Italy.

Maria Luisa Dupuis (ML)

Center for Gender Specific Medicine, Istituto Superiore di Sanità, Rome, Italy.

Eleonora Petrucci (E)

Department of Oncology and Molecular Medicine, Istituto Superiore di Sanità, Rome, Italy.

Roberta Riccioni (R)

Department of Oncology and Molecular Medicine, Istituto Superiore di Sanità, Rome, Italy.

Mauro Andreotti (M)

National Center for Global Health, Istituto Superiore di Sanità, Rome, Italy.

Carla Raggi (C)

National Center for Control and Evaluation of Medicine, Istituto Superiore di Sanità, Rome, Italy.

Alessandra Boe (A)

Core Facilities, Istituto Superiore di Sanità, Rome, Italy.

Stefano Barca (S)

National Center for Drug Research and Evaluation Unit of Preclinical and Clinical Evaluation of Medicinal Drugs, Istituto Superiore di Sanità, Rome, Italy.

Mara Gellini (M)

National Center for Global Health, Istituto Superiore di Sanità, Rome, Italy.

Stefano Vella (S)

National Center for Global Health, Istituto Superiore di Sanità, Rome, Italy.

Alessandra Mallano (A)

National Center for Global Health, Istituto Superiore di Sanità, Rome, Italy.

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Classifications MeSH