Studies on the Escape Mutants of Rabies Virus Which Are Resistant to Neutralization by a Highly Conserved Conformational Epitope‐Specific Monoclonal Antibody #1‐46‐12

Irie, Takashi; Matsuda, Yukihiro; Honda, Yoshikazu; Morimoto, Kanehisa; Kawai, Akihiko

doi:10.1111/j.1348-0421.2002.tb02719.x

Cited by 13 publications

(37 citation statements)

References 28 publications

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“…The sequon at Asn 158 was detected in the fixed virus strain HEP-Flury, which was established by serial passaging in chicken eggs. Irie et al (2002) found that baby hamster kidney (BHK)-21 cell-adapted HEP-Flury lost the sequon at Asn 158 . Therefore, the facilitative effect of the N-glycan at Asn 158 on virus production might be cell-type specific, although the mechanism is unknown.…”

mentioning

confidence: 99%

Addition of a single N-glycan to street rabies virus glycoprotein enhances virus production

Yamada

Noguchi

Nonaka

et al. 2013

Journal of General Virology

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Most street rabies virus G proteins have two N-glycosylation sites, i.e. Asn37 and Asn319, whereas additional sites are found in fixed (laboratory adapted) viruses. In this study, we performed a pseudotyped virus assay using G-deficient rabies virus and demonstrated that single-N-glycan additions to the G protein of street rabies virus strain 1088, which are found in adapted strains, enhanced virus production in neural and non-neural cell lines, while additions to Asn194 or Asn247 enhanced production greatly. Moreover, we found that N-glycan additions at Asn194 or Asn247 facilitated the production of cell-associated virus. In contrast, deletion of the sequon at Asn37 reduced viral production, while a deletion at Asn319 resulted in extensive loss of production. Furthermore, G proteins lacking an N-glycan at Asn319 failed to fold into their correct structure and lost their fusion activity, indicating that Asn319 N-glycosylation is important for the functional expression of street virus G proteins.

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mentioning

confidence: 99%

Addition of a single N-glycan to street rabies virus glycoprotein enhances virus production

Yamada

Noguchi

Nonaka

et al. 2013

Journal of General Virology

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“…In present study, culture fluids of the hybridoma cells were mostly used as the mAb source. Antibody concentration of each mAb stock was estimated by semi-quantitative immunoblot assay using a mouse immunoglobulin sample of known concentration and peroxidase-conjugated anti-mouse goat antibody (Cappel) as described previously (15). Hybridoma culture fluids contained about 10 µg protein/ml of the antibody, which was sufficient for this study.…”

Section: Methodsmentioning

confidence: 99%

“…For sequencing of the G gene of mutant viruses, G cDNAs fragments were prepared from the virion RNA by an RT-PCR method using the set of primers described in our previous report (15). The first strand of G cDNA was prepared using the viral genome RNA as the template of reversetranscription by AMV reverse transcriptase, and then amplified by PCR with Taq DNA polymerase (ExTaq, TaKaRa; 23).…”

Section: Methodsmentioning

confidence: 99%

“…After three passages, ten virus isolates (#13044R-301 to -310) were obtained from the plaques formed on BHK-21 cell sheets, amplified in BHK-21 cell cultures, and checked for their sensitivity to the mAb. The antibody-resistant clones were next subjected to RT-PCR (reverse transcription-polymerase chain reaction) to examine the G gene sequence using the same primers described previously (15).…”

Section: Methodsmentioning

confidence: 99%

“…In our recent study (15), mAb #1-30-44 was shown to recognize most laboratory strains of the rabies virus, while the CVS strain lacked the epitope. Accordingly, we planned to map the 1-30-44 epitope on the G protein molecule using the two cDNA clones encoding the HEPFlury and CVS G proteins.…”

Section: ) Mapping Of the #1-30-44 Epitopementioning

confidence: 99%

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Mapping of the Low pH‐Sensitive Conformational Epitope of Rabies Virus Glycoprotein Recognized by a Monoclonal Antibody #1‐30‐44

Kankanamge

Irie

Mannen

et al. 2003

Microbiology and Immunology

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Monoclonal antibody (mAb) #1‐30‐44 recognized an acid‐sensitive conformational epitope of rabies virus glycoprotein (G). The antigenicity of G protein exposed on the cell surface was lost when the infected cells were exposed to pH 5.8. By comparing the deduced amino acid sequence of G protein between the HEP‐Flury strain and the epitope‐negative CVS strain as well as the mAb‐resistant escape mutants, two distant sites that contained Lys‐202 and Asn‐336 were shown to be involved in the epitope formation. Lys‐202 is located in the so‐called neurotoxin‐like sequence, while Asn‐336 is included in antigenic site III and is very near the amino acid at position 333, which is known to affect greatly the neuropathogenicity of rabies virus when changed. Consistent with this finding, antigenicity of a neurovirulent revertant of the HEP‐Flury strain, in which Gln‐333 of G protein was replaced by Arg, was also affected as shown by its greatly decreased reactivity with mAb #1‐30‐44 compared to that of the original avirulent HEP virus. Based on these results, we hypothesize that the neurotoxin‐like domain and some amino acids in antigenic site III come into contact with each other to form a conformational epitope for mAb #1‐30‐44, and such a configuration would be lost when exposed to acidic conditions to perform a certain low pH‐dependent function of G protein.

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One-dose intradermal rabies booster enhances rabies antibody production and avidity maturation

Kewcharoenwong,

Freeouf,

Nithichanon

et al. 2024

Med Microbiol Immunol

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The incidence of rabies in Thailand reached its peak in 2018 with 18 human deaths. Preexposure prophylaxis (PrEP) vaccination is thus recommended for high-risk populations. WHO has recently recommended that patients who are exposed to a suspected rabid animal and have already been immunized against rabies should receive a 1-site intradermal (ID) injection of 0.1 mL on days 0 and 3 as postexposure prophylaxis (PEP). In Thailand, village health and livestock volunteers tasked with annual dog vaccination typically receive only a single lifetime PrEP dose and subsequent boosters solely upon confirmed animal bites. However, the adequacy of a single PrEP dose for priming and maintaining immunity in this high-risk group has not been evaluated. Therefore, our study was designed to address two key questions: (1) sufficiency of single-dose PrEP—to determine whether a single ID PrEP dose provides adequate long-term immune protection for high-risk individuals exposed to numerous dogs during their vaccination duties. (2) Booster efficacy for immune maturation—to investigate whether one or two additional ID booster doses effectively stimulate a mature and sustained antibody response in this population. The level and persistence of the rabies antibody were determined by comparing the immunogenicity and booster efficacy among the vaccination groups. Our study demonstrated that rabies antibodies persisted for more than 180 days after cost-effective ID PrEP or the 1st or the 2nd single ID booster dose, and adequate antibody levels were detected in more than 95% of participants by CEE-cELISA and 100% by indirect ELISA. Moreover, the avidity maturation of rabies-specific antibodies occurred after the 1st single ID booster dose. This smaller ID booster regimen was sufficient for producing a sufficient immune response and enhancing the maturation of anti-rabies antibodies. This safe and effective PrEP regimen and a single visit involving a one-dose ID booster are recommended, and at least one one-dose ID booster regimen could be equitably implemented in at-risk people in Thailand and other developing countries. However, an adequate antibody level should be monitored before the booster is administered.

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Studies on the Escape Mutants of Rabies Virus Which Are Resistant to Neutralization by a Highly Conserved Conformational Epitope‐Specific Monoclonal Antibody #1‐46‐12

Cited by 13 publications

References 28 publications

Addition of a single N-glycan to street rabies virus glycoprotein enhances virus production

Addition of a single N-glycan to street rabies virus glycoprotein enhances virus production

Mapping of the Low pH‐Sensitive Conformational Epitope of Rabies Virus Glycoprotein Recognized by a Monoclonal Antibody #1‐30‐44

One-dose intradermal rabies booster enhances rabies antibody production and avidity maturation

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