A monoclonal antibody recognizing a new epitope on CD81 inhibits T-cell migration without inducing cytokine production

Author:

Hasezaki Takuya1,Yoshima Tadahiko2,Mattsson Mikael3,Särnefält Anna3,Takubo Keiko4

Affiliation:

1. External Innovation, Sumitomo Dainippon Pharma Co., Ltd, 3-1-98 Kasugade Naka, Konohana-ku, Osaka 554-0022, Japan

2. Applied Bioscience Group, Bioscience Research Laboratory, Sumitomo Chemical Co., Ltd, 3-1-98 Kasugade Naka, Konohana-ku, Osaka 554-0022, Japan

3. BioInvent International AB, Sölvegatan 41, SE-223 70 Lund, Sweden

4. Group II, Platform Technology Research Unit, Sumitomo Dainippon Pharma Co., Ltd, 3-1-98 Kasugade Naka, Konohana-ku, Osaka 554-0022, Japan

Abstract

AbstractCD81 is involved in leukocyte migration and cytokine induction. Previous work found that anti-CD81 monoclonal antibodies (mAbs) showed therapeutic potential for several immune diseases via inhibiting leukocyte migration. Although the suppression of cell migration is a promising approach for treating immune diseases, some anti-CD81 mAbs can induce cytokine production, which may exacerbate disease. To obtain new anti-human CD81 mAbs that inhibited migration in the absence of cytokine production enhancement activity, we screened a human single chain variable fragment by phage library. One of the new anti-CD81 mAbs isolated, DSP-8250, had equivalent inhibitory cell migration activity with the established anti-CD81 mAb 5A6, but it lacked cytokine induction activity. These mAbs recognized different epitopes on CD81. mAb 5A6, which had inhibitory activity on T-cell migration and increased cytokine production, bound to three residues, Ser179, Asn180 and Phe186 of CD81. In contrast, DSP-8250, which had inhibitory activity on T-cell migration but no cytokine enhancement activity, bound to four residues, His151, Ala164, Ser168 and Asn172 of CD81 as a unique epitope. These results indicate that the set of His151, Ala164, Ser168 and Asn172 forms a novel epitope that might make the application of anti-CD81 mAb therapeutically useful.

Funder

Sumitomo Dainippon Pharma. Co. Ltd.

Publisher

Oxford University Press (OUP)

Subject

Molecular Biology,Biochemistry,General Medicine

Reference40 articles.

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