The generation of the human mab RabD4 specific to the rabies virus glycoprotein and characterization thereof

We generated a novel human neutralizing human mAb RabD4 against rabies virus glycoprotein using in vitro stimulation human peripheral B cells produced from immunized donor. It was revealed that the human mAb RabD4 demonstrated high antigen-binding activity and virus-neutralizing activity in the FAVN test with the CVS-11 rabies virus.

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Investigation of rabies virus glycoprotein carboxyl terminus as an in vitro predictive tool of neurovirulence. A 3R approach

Microbes and Infection ◽

10.1016/j.micinf.2017.05.006 ◽

2017 ◽

Vol 19 (9-10) ◽

pp. 476-484 ◽

Cited By ~ 4

Author(s):

Wonhyo Seo ◽

Christophe Prehaud ◽

Zakir Khan ◽

Claude Sabeta ◽

Monique Lafon

Keyword(s):

Rabies Virus ◽

Carboxyl Terminus ◽

Predictive Tool ◽

Rabies Virus Glycoprotein ◽

Virus Glycoprotein

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Standardization of an enzyme immunoassay for the in vitro potency assay of inactivated tissue culture rabies vaccines: determination of the rabies virus glycoprotein with polyclonal antisera

Journal of Biological Standardization ◽

10.1016/s0092-1157(89)80001-0 ◽

1989 ◽

Vol 17 (4) ◽

pp. 291-309 ◽

Cited By ~ 19

Author(s):

Olaf Thraenhart ◽

Kandiah Ramakrishnan

Keyword(s):

Tissue Culture ◽

Enzyme Immunoassay ◽

Rabies Virus ◽

Potency Assay ◽

Rabies Virus Glycoprotein ◽

Virus Glycoprotein ◽

Polyclonal Antisera

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The Rabies Virus Glycoprotein Receptor p75NTR Is Not Essential for Rabies Virus Infection

Journal of Virology ◽

10.1128/jvi.02368-06 ◽

2007 ◽

Vol 81 (24) ◽

pp. 13622-13630 ◽

Cited By ~ 50

Author(s):

Christine Tuffereau ◽

Klaus Schmidt ◽

Christelle Langevin ◽

Florence Lafay ◽

Georg Dechant ◽

...

Keyword(s):

Virus Infection ◽

Rabies Virus ◽

Neurotrophin Receptor ◽

Virus Infectivity ◽

Primary Neurons ◽

Drg Neurons ◽

Rabies Virus Glycoprotein ◽

Virus Glycoprotein

ABSTRACT Rabies virus glycoprotein (RVG) is known to be the only factor that mediates rabies infection. The neurotrophin receptor (p75NTR), through its cysteine-rich domain 1, is a specific receptor for RVG and neutralizes virus infectivity, but its role in virus infection has remained obscure. We used adult mouse dorsal root ganglion (DRG) neurons as a model to study the role of p75NTR in RV infection of primary neurons. We show that RV infects around 20% of DRG neurons, of which more than 80% are p75NTR positive, have large diameters, and are capsaicin insensitive. Surprisingly, RV binding and infection are absent in about half of the p75NTR-expressing DRG neurons which have small diameters and are often capsaicin sensitive. This indicates that p75NTR is not sufficient to mediate RV interaction in sensory neurons. The rate and specificity of neural infection are unchanged in RV-infected p75NTRExonIV−/− mice that lack all extracellular receptor domains and in wild-type mice infected with two independent RV mutants that lack p75NTR binding. Accordingly, the mortality rate is unchanged in the absence of RV-p75NTR interaction. We conclude that although p75NTR is a receptor for soluble RVG in transfected cells of heterologous expression systems, an RVG-p75NTR interaction is not necessary for RV infection of primary neurons. This means that other receptors are required to mediate RV infection in vivo and in vitro.

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