Alexey Y. Sazykin

Lomonosov Moscow State University

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Pavel V. Belousov

Endocrinology Research Center

Dmitry V. Kuprash

Engelhardt Institute of Molecular Biology

Sergei A. Nedospasov

Lomonosov Moscow State University

Svetlana V. Khlgatian

Research Institute of Vaccines and Sera. Mechnikov of the Russian Academy of Medical Sciences

Ekaterina P. Koroleva

The University of Texas Health Science Center at San Antonio

Yuriy V. Shebzukhov

German Rheumatism Research Centre

Dmitry Penkov

National Medical Research Center of Cardiology

David Eisel

BioNTech (Germany)

Verona Vass

Friedrich-Alexander-Universität Erlangen-Nürnberg

Stefan Stevanović

University of Tübingen

Cooperative Institutions

Engelhardt Institute of Molecular Biology

Lomonosov Moscow State University

Russian Academy of Sciences

German Rheumatism Research Centre

Immatics Biotechnologies (Germany)

Moscow State University

University of Tübingen

Ministry of Health of the Russian Federation

German Cancer Research Center

Heidelberg University

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Supplementary Figure 1 from Alternative Variants of Human HYDIN Are Novel Cancer-Associated Antigens Recognized by Adaptive Immunity

Karoline Laske Yuriy V. Shebzukhov Ludger Große‐Hovest Dmitry V. Kuprash Svetlana V. Khlgatian

PDF - 395KB, Supplementary Figure 1: Structure of MO-TES391 and KIAA1864 transcripts.

10.1158/2326-6066.22537066.v1

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Supplementary Figure 1 from Alternative Variants of Human HYDIN Are Novel Cancer-Associated Antigens Recognized by Adaptive Immunity

Karoline Laske Yuriy V. Shebzukhov Ludger Große‐Hovest Dmitry V. Kuprash Svetlana V. Khlgatian

PDF - 395KB, Supplementary Figure 1: Structure of MO-TES391 and KIAA1864 transcripts.

10.1158/2326-6066.22537066

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Search for alternative platforms for Caspase-2 activation upon genotoxic stress

Gelina S. Kopeina Alexey V. Zamaraev Alexey Y. Sazykin V.A. Radyukhin Inna N. Lavrik

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Supplementary Table 3 from Alternative Variants of Human HYDIN Are Novel Cancer-Associated Antigens Recognized by Adaptive Immunity

Karoline Laske Yuriy V. Shebzukhov Ludger Große‐Hovest Dmitry V. Kuprash Svetlana V. Khlgatian

PDF - 49KB, Supplementary Table 3: Epitope prediction for HLA-A*02 binding peptides derived from KIAA1864 and MO-TES391.

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10.1158/2326-6066.22537051.v1

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Supplementary Figure Legends from Alternative Variants of Human HYDIN Are Novel Cancer-Associated Antigens Recognized by Adaptive Immunity

Karoline Laske Yuriy V. Shebzukhov Ludger Große‐Hovest Dmitry V. Kuprash Svetlana V. Khlgatian

PDF - 88KB, Supplementary Figure Legends.

10.1158/2326-6066.22537060

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Alternative Variants of Human HYDIN Are Novel Cancer-Associated Antigens Recognized by Adaptive Immunity

Cancer Immunology Research (2013)

Karoline Laske Yuriy V. Shebzukhov Ludger Große‐Hovest Dmitry V. Kuprash Svetlana V. Khlgatian

A mutation in the hydin gene has been recently described as one possible mechanism leading to lethal congenital hydrocephalus in mice, and a similar defect is proposed to be involved in an autosomal recessive form of hydrocephalus in human. Here, we report for the first time on the cancer association and immunogenicity of two HYDIN variants in humans. One is a previously described sequence derived from the chromosome 1 gene copy, that is, KIAA1864. The second is encoded by a novel alternative transcript originating from the chromosome 16, which we identified by immunoscreening of a testis-derived cDNA expression library with sera of patients with colorectal cancer, and called MO-TES391. Both variants are targeted by immunoglobulin G antibodies in a significant subset of cancer patients but only rarely in healthy donors. Moreover, we identify HLA-A*0201-restricted sequences derived from MO-TES391 and KIAA1864, which are specifically recognized by human cytotoxic CD8(+) T cells. Taken together, these results suggest frequent and coordinated adaptive immune responses against HYDIN variants in patients with cancer and propose HYDIN as a novel cancer-associated antigen.

10.1158/2326-6066.cir-13-0079

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Supplementary Table 1 from Alternative Variants of Human HYDIN Are Novel Cancer-Associated Antigens Recognized by Adaptive Immunity

Karoline Laske Yuriy V. Shebzukhov Ludger Große‐Hovest Dmitry V. Kuprash Svetlana V. Khlgatian

PDF - 60KB, Supplementary Table 1: Serological reactivity of MO-TES391 assessed by SMARTA.

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10.1158/2326-6066.22537057

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Supplementary Table 1 from Alternative Variants of Human HYDIN Are Novel Cancer-Associated Antigens Recognized by Adaptive Immunity

Karoline Laske Yuriy V. Shebzukhov Ludger Große‐Hovest Dmitry V. Kuprash Svetlana V. Khlgatian

PDF - 60KB, Supplementary Table 1: Serological reactivity of MO-TES391 assessed by SMARTA.

Table (database)

10.1158/2326-6066.22537057.v1

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DETECTION OF AUTOANTIBODIES RECOGNIZING CANCERRETINA ANTIGEN RECOVERIN IN BLOOD OF PATIENTS WITH NON-INVASIVE FOLLICULAR THYROID NEOPLASMS WITH PAPILLARY-LIKE NUCLEAR FEATURES (NIFTP)

Medical Immunology (Russia) (2019)

Pavel V. Belousov Ya. I. Bobrovskaya A. V. Bogolyubova Alexey Y. Sazykin Yu. V. Shebzukhov

Autoantibodies recognizing the cancer-retina autoantigen called recoverin (RCVRN-AutoAb) may serve as a highly specific biomarker of cancer-associated retinopathy. However, they may also be found in some cancer patients without clinical evidence of retinopathy. In the present study, dot-ELISA and Western blot assays were used to demonstrate the presence of circulating RCVRN-AutoAb in 4/7 (57%) of patients with recently recognized pathological entity, non-invasive follicular thyroid neoplasm with papillary-like nuclear features (NIFTP); other thyroid tumors represented by follicular adenomas, and classical and follicular variants of papillary thyroid carcinomas, demonstrated low frequencies of RCVRN-AutoAb (0/15, 1/20 (5%) and 1/15 (7%), respectively), with no significant differences from healthy individuals (0/15). Our data implicate the circulating RCVRN-AutoAb as a potential biomarker of NIFTP capable of discrimination of this novel pathological entity from other thyroid tumors.

Recoverin

Thyroid neoplasm

10.15789/1563-0625-2019-4-781-788

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Citations (1)

[Preparation of immunoenzyme conjugates of beta-lactamase from Bacillus licheniformis 749/c and horseradish peroxidase with human antibodies to HIV-1].

PubMed (1991)

Alexey Y. Sazykin С. А. Еремин А.М. Егоров A. V. Starov I. Sakayan

By using three different linkage methods with carbodiimide, glutaraldehyde and periodite, immunoenzyme conjugates of beta-lactamase from Bacillus licheniformis 749/c and horse radish peroxidase with human antibodies to HIV-1 were prepared. The human antibodies were purified by the affinity procedure on Protein-A-Sepharose 6B. The conjugates were tested in a solid phase immunoenzymatic system for the HIV-1 antigen. It was shown that the conjugates prepared by the carbodiimide linkage method had the highest titer, the beta-lactamase conjugate being superior by its titer to the respective peroxidase conjugate. In the lyophilized state the conjugates prepared with the carbodiimide linkage method were stable.

Carbodiimide

Conjugate

Horseradish peroxidase

Glutaraldehyde

Bacillus licheniformis

Sepharose

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