Determination of the antigen/epitope that is recognized by human monoclonal antibody CLN-IgG

Hagiwara, Hideaki; Aotsuka, Yasuyuki; Yamämoto, Yasushi; Miyahara, Junichi; Mitoh, Yuko

doi:10.3233/hab-2001-10204

Cited by 12 publications

(8 citation statements)

References 11 publications

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“…The antigen recognized by pritumumab is a "vimentin-like" protein [19,42]. The sequence of the antigen is in homology with the vimentin gene but the neo-epitope recognized by pritumumab is novel in that it is expressed on the cell surface [42] and does not match the specificity of commercially available antivimentin antibodies. It was speculated that the natural human immune response recognized the vimentin-like neo-epitope when it became expressed on the surface of malignant epithelial cells.…”

Section: Discussionmentioning

confidence: 99%

“…Sequence analysis of purified antigen showed it to be altered vimentin [19,42]. The reactive epitope is located in the c2 (coil 2 of the central rod) domain of vimentin [42]. The antigen was found to be cell bound and not circulating either in the serum or cerebrospinal fluid [32].…”

Section: Antigen Characterizationmentioning

confidence: 99%

“…Reference Clone generation [3] Specificity analysis [3,4,9,16,17,25] Effector functions [14][15][16][17][18] Xenograft model [17,41] Antigen characterization [19,42] ent human hybridoma, CLNH11 [3,4]. The general properties of pritumumab antibody are listed in Table 1 with their respective reference.…”

Section: Propertymentioning

confidence: 99%

“…Scatchard analysis showed a pritumumab affinity of 4.5 × 10 −7 M with the antigen from U-251MG cells. Sequence analysis of purified antigen showed it to be altered vimentin [19,42]. The reactive epitope is located in the c2 (coil 2 of the central rod) domain of vimentin [42].…”

Section: Antigen Characterizationmentioning

confidence: 99%

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Summary analysis of the pre-clinical and clinical results of brain tumor patients treated with pritumumab

Glassy

Hagiwara²

2009

HAB

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Pritumumab is a human IgG1 kappa antibody that has been derived from a B-cell isolated from a regional draining lymph node of a patient with cervical carcinoma. Specificity analysis of the antibody with human tissues showed the antigen, altered tumor-associated vimentin, to be highly restricted to various cancers and not normal cells and tissues. In various clinical trials in Japan 249 patients with brain cancer were treated with pritumumab. The overall response rate was between 25-30% with several survivors beyond 5-years post-treatment. The patients were on a low dose regimen of 1mg given twice a week for a course of 24 weeks for a total dose of 48 mgs per course. Pritumumab appears to be a safe and effective therapy in patients with malignant gliomas.

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Section: Discussionmentioning

confidence: 99%

Section: Antigen Characterizationmentioning

confidence: 99%

Section: Propertymentioning

confidence: 99%

Section: Antigen Characterizationmentioning

confidence: 99%

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Summary analysis of the pre-clinical and clinical results of brain tumor patients treated with pritumumab

Glassy

Hagiwara²

2009

HAB

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“…I am still wondering how these remarkable responses to brain tumors was evoked in the course of CLN-IgG Pritumumab-tumor antigen specific immunotherapy. The tumor associated antigen (TA226) recognized by CLN-IgG was vimentin and the epitope was expressed in a sequence of 79 amino acids (aa) in vimentin coil 2B [2]. The sequence of vimentin-epitope79 was the same between malignant and normal cells.…”

mentioning

confidence: 99%

On the Dichotomous Aspect of Cancer Stem Cell

Av¹

2018

OAJCO

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Extracellular Vimentin as a Target Against SARS‐CoV‐2 Host Cell Invasion

Suprewicz

Swoger

Gupta

et al. 2021

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Infection of human cells by pathogens, including SARS‐CoV‐2, typically proceeds by cell surface binding to a crucial receptor. The primary receptor for SARS‐CoV‐2 is the angiotensin‐converting enzyme 2 (ACE2), yet new studies reveal the importance of additional extracellular co‐receptors that mediate binding and host cell invasion by SARS‐CoV‐2. Vimentin is an intermediate filament protein that is increasingly recognized as being present on the extracellular surface of a subset of cell types, where it can bind to and facilitate pathogens’ cellular uptake. Biophysical and cell infection studies are done to determine whether vimentin might bind SARS‐CoV‐2 and facilitate its uptake. Dynamic light scattering shows that vimentin binds to pseudovirus coated with the SARS‐CoV‐2 spike protein, and antibodies against vimentin block in vitro SARS‐CoV‐2 pseudovirus infection of ACE2‐expressing cells. The results are consistent with a model in which extracellular vimentin acts as a co‐receptor for SARS‐CoV‐2 spike protein with a binding affinity less than that of the spike protein with ACE2. Extracellular vimentin may thus serve as a critical component of the SARS‐CoV‐2 spike protein‐ACE2 complex in mediating SARS‐CoV‐2 cell entry, and vimentin‐targeting agents may yield new therapeutic strategies for preventing and slowing SARS‐CoV‐2 infection.

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Determination of the antigen/epitope that is recognized by human monoclonal antibody CLN-IgG

Cited by 12 publications

References 11 publications

Summary analysis of the pre-clinical and clinical results of brain tumor patients treated with pritumumab

Summary analysis of the pre-clinical and clinical results of brain tumor patients treated with pritumumab

On the Dichotomous Aspect of Cancer Stem Cell

Extracellular Vimentin as a Target Against SARS‐CoV‐2 Host Cell Invasion

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