» Articles » PMID: 18066039

The Growth and Potential of Human Antiviral Monoclonal Antibody Therapeutics

Overview
Journal Nat Biotechnol
Specialty Biotechnology
Date 2007 Dec 11
PMID 18066039
Citations 141
Authors
Affiliations
Soon will be listed here.
Abstract

Monoclonal antibodies (mAbs) have long provided powerful research tools for virologists to understand the mechanisms of virus entry into host cells and of antiviral immunity. Even so, commercial development of human (or humanized) mAbs for the prophylaxis, preemptive and acute treatment of viral infections has been slow. This is surprising, as new antibody discovery tools have increased the speed and precision with which potent neutralizing human antiviral mAbs can be identified. As longstanding barriers to antiviral mAb development, such as antigenic variability of circulating viral strains and the ability of viruses to undergo neutralization escape, are being overcome, deeper insight into the mechanisms of mAb action and engineering of effector functions are also improving the efficacy of antiviral mAbs. These successes, in both industrial and academic laboratories, coupled with ongoing changes in the biomedical and regulatory environments, herald an era when the commercial development of human antiviral mAb therapies will likely surge.

Citing Articles

Recent Advances in Immunological Landscape and Immunotherapeutic Agent of Nipah Virus Infection.

Chakraborty C, Saha S, Bhattacharya M Cell Biochem Biophys. 2024; 82(4):3053-3069.

PMID: 39052192 DOI: 10.1007/s12013-024-01424-4.


AttABseq: an attention-based deep learning prediction method for antigen-antibody binding affinity changes based on protein sequences.

Jin R, Ye Q, Wang J, Cao Z, Jiang D, Wang T Brief Bioinform. 2024; 25(4).

PMID: 38960407 PMC: 11221889. DOI: 10.1093/bib/bbae304.


A broadly neutralizing human monoclonal antibody generated from transgenic mice immunized with HCMV particles limits virus infection and proliferation.

Atanasoff K, Parsons A, Ophir S, Lurain N, Kraus T, Moran T J Virol. 2024; 98(7):e0021324.

PMID: 38832789 PMC: 11264687. DOI: 10.1128/jvi.00213-24.


Single domain antibodies from camelids in the treatment of microbial infections.

De Greve H, Fioravanti A Front Immunol. 2024; 15:1334829.

PMID: 38827746 PMC: 11140111. DOI: 10.3389/fimmu.2024.1334829.


A synergistic therapy against influenza virus A/H1N1/PR8 by a HA1 specific neutralizing single-domain V and an RNA hydrolyzing scFv.

Hoang P, Luong Q, Ayun R, Lee Y, Oh K, Kim T Front Microbiol. 2024; 15:1355599.

PMID: 38706966 PMC: 11066198. DOI: 10.3389/fmicb.2024.1355599.


References
1.
Heinz F . Epitope mapping of flavivirus glycoproteins. Adv Virus Res. 1986; 31:103-68. DOI: 10.1016/s0065-3527(08)60263-8. View

2.
Jacobson J, Colman N, Ostrow N, Simson R, Tomesch D, Marlin L . Passive immunotherapy in the treatment of advanced human immunodeficiency virus infection. J Infect Dis. 1993; 168(2):298-305. DOI: 10.1093/infdis/168.2.298. View

3.
Sloan S, Hanlon C, Weldon W, Niezgoda M, Blanton J, Self J . Identification and characterization of a human monoclonal antibody that potently neutralizes a broad panel of rabies virus isolates. Vaccine. 2007; 25(15):2800-10. DOI: 10.1016/j.vaccine.2006.12.031. View

4.
Gilmour J . Expression of neutralizing recombinant human antibodies against Varicella Zoster virus for use as a potential prophylactic. Hybridoma. 2000; 19(2):143-9. DOI: 10.1089/02724570050031185. View

5.
Burton D, Desrosiers R, Doms R, Koff W, Kwong P, Moore J . HIV vaccine design and the neutralizing antibody problem. Nat Immunol. 2004; 5(3):233-6. DOI: 10.1038/ni0304-233. View