TY  - JOUR
N1  - Open Access
ID  - open1900
UR  - http://www.nature.com/articles/srep21240
A1  - Sankhyan, Anurag
A1  - Sharma, Chandresh
A1  - Dutta, Durgashree
A1  - Sharma, Tarang
A1  - Chosdol, Kunzang
A1  - Wakita, Takaji
A1  - Watashi, Koichi
A1  - Awasthi, Amit
A1  - Acharya, Subrat K
A1  - Khanna, Navin
A1  - Tiwari, Ashutosh
A1  - Sinha, Subrata
Y1  - 2016///
N2  - Neutralizing monoclonal antibodies are being found to be increasingly useful in viral infections. In hepatitis B infection, antibodies are proven to be useful for passive prophylaxis. The preS1 region (21-47a.a.) of HBV contains the viral hepatocyte-binding domain crucial for its attachment and infection of hepatocytes. Antibodies against this region are neutralizing and are best suited for immune-based neutralization of HBV, especially in view of their not recognizing decoy particles. Anti-preS1 (21-47a.a.) antibodies are present in serum of spontaneously recovered individuals. We generated a phage-displayed scFv library using circulating lymphocytes from these individuals and selected four preS1-peptide specific scFvs with markedly distinct sequences from this library. All the antibodies recognized the blood-derived and recombinant preS1 containing antigens. Each scFv showed a discrete binding signature, interacting with different amino acids within the preS1-peptide region. Ability to prevent binding of the preS1 protein (N-terminus 60a.a.) to HepG2 cells stably expressing hNTCP (HepG2-hNTCP-C4 cells), the HBV receptor on human hepatocytes was taken as a surrogate marker for neutralizing capacity. These antibodies inhibited preS1-hepatocyte interaction individually and even better in combination. Such a combination of potentially neutralizing recombinant antibodies with defined specificities could be used for preventing/managing HBV infections, including those by possible escape mutants.
PB  - NPG
JF  - Scientific reports
VL  - 6
KW  - Antibody therapy; Transnational immunology

SN  - 2045-2322
TI  - Inhibition of preS1-hepatocyte interaction by an array of recombinant human antibodies from naturally recovered individuals.
ER  -