Identification of novel interferon responsive protein partners
of human leukocyte antigen A (HLA-A) using cross-linking mass
spectrometry (CLMS) approach

J 2022

Identification of novel interferon responsive protein partners of human leukocyte antigen A (HLA-A) using cross-linking mass spectrometry (CLMS) approach

SINGH, Ashita; Monikaben PADARIYA; Jakub FAKTOR; Sachin KOTE; Sara MIKAC et al.

Základní údaje

Originální název

Identification of novel interferon responsive protein partners of human leukocyte antigen A (HLA-A) using cross-linking mass spectrometry (CLMS) approach

Autoři

Vydání

Scientific Reports, Nature Research, 2022, 2045-2322

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10608 Biochemistry and molecular biology

Stát vydavatele

Německo

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 4.600

Označené pro přenos do RIV

Ano

Kód RIV

RIV/00216224:14310/22:00128367

Organizační jednotka

Přírodovědecká fakulta

Klíčová slova anglicky

cancer; HLA-A; cross-linking mass spectrometry; proteins

Štítky

14314010, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 30. 1. 2023 14:53, Mgr. Marie Novosadová Šípková, DiS.

Anotace

V originále

The interferon signalling system elicits a robust cytokine response against a wide range of environmental pathogenic and internal pathological signals, leading to induction of a subset of interferon-induced proteins. We applied DSS (disuccinimidyl suberate) mediated cross-linking mass spectrometry (CLMS) to capture novel protein–protein interactions within the realm of interferon induced proteins. In addition to the expected interferon-induced proteins, we identified novel inter- and intra-molecular cross-linked adducts for the canonical interferon induced proteins, such as MX1, USP18, OAS3, and STAT1. We focused on orthogonal validation of a cohort of novel interferon-induced protein networks formed by the HLA-A protein (H2BFS-HLA-A-HMGA1) using co-immunoprecipitation assay, and further investigated them by molecular dynamics simulation. Conformational dynamics of the simulated protein complexes revealed several interaction sites that mirrored the interactions identified in the CLMS findings. Together, we showcase a proof-of-principle CLMS study to identify novel interferon-induced signaling complexes and anticipate broader use of CLMS to identify novel protein interaction dynamics within the tumour microenvironment.

Citovat

SINGH, Ashita; Monikaben PADARIYA; Jakub FAKTOR; Sachin KOTE; Sara MIKAC; Alicja DZIADOSZ; Tak W LAM; Jack BRYDON; Martin A WEAR; Kathryn L BALL; Ted HUPP; Alicja SZNARKOWSKA; Borek VOJTESEK a Umesh KALATHIYA. Identification of novel interferon responsive protein partners of human leukocyte antigen A (HLA-A) using cross-linking mass spectrometry (CLMS) approach. Scientific Reports. Nature Research, 2022, roč. 12, č. 1, s. 1-16. ISSN 2045-2322. Dostupné z: https://doi.org/10.1038/s41598-022-21393-z.

@article{2251026,
   author = {Singh, Ashita and Padariya, Monikaben and Faktor, Jakub and Kote, Sachin and Mikac, Sara and Dziadosz, Alicja and Lam, Tak W and Brydon, Jack and Wear, Martin A and Ball, Kathryn L and Hupp, Ted and Sznarkowska, Alicja and Vojtesek, Borek and Kalathiya, Umesh},
   article_number = {1},
   doi = {https://doi.org/10.1038/s41598-022-21393-z},
   keywords = {cancer; HLA-A; cross-linking mass spectrometry; proteins},
   language = {eng},
   issn = {2045-2322},
   journal = {Scientific Reports},
   title = {Identification of novel interferon responsive protein partners of human leukocyte antigen A (HLA-A) using cross-linking mass spectrometry (CLMS) approach},
   url = {https://doi.org/10.1038/s41598-022-21393-z},
   volume = {12},
   year = {2022}
}

TY  - JOUR
ID  - 2251026
AU  - Singh, Ashita - Padariya, Monikaben - Faktor, Jakub - Kote, Sachin - Mikac, Sara - Dziadosz, Alicja - Lam, Tak W - Brydon, Jack - Wear, Martin A - Ball, Kathryn L - Hupp, Ted - Sznarkowska, Alicja - Vojtesek, Borek - Kalathiya, Umesh
PY  - 2022
TI  - Identification of novel interferon responsive protein partners of human leukocyte antigen A (HLA-A) using cross-linking mass spectrometry (CLMS) approach
JF  - Scientific Reports
VL  - 12
IS  - 1
SP  - 1-16
EP  - 1-16
PB  - Nature Research
SN  - 20452322
KW  - cancer
KW  - HLA-A
KW  - cross-linking mass spectrometry
KW  - proteins
UR  - https://doi.org/10.1038/s41598-022-21393-z
N2  - The interferon signalling system elicits a robust cytokine response against a wide range of environmental pathogenic and internal pathological signals, leading to induction of a subset of interferon-induced proteins. We applied DSS (disuccinimidyl suberate) mediated cross-linking mass spectrometry (CLMS) to capture novel protein–protein interactions within the realm of interferon induced proteins. In addition to the expected interferon-induced proteins, we identified novel inter- and intra-molecular cross-linked adducts for the canonical interferon induced proteins, such as MX1, USP18, OAS3, and STAT1. We focused on orthogonal validation of a cohort of novel interferon-induced protein networks formed by the HLA-A protein (H2BFS-HLA-A-HMGA1) using co-immunoprecipitation assay, and further investigated them by molecular dynamics simulation. Conformational dynamics of the simulated protein complexes revealed several interaction sites that mirrored the interactions identified in the CLMS findings. Together, we showcase a proof-of-principle CLMS study to identify novel interferon-induced signaling complexes and anticipate broader use of CLMS to identify novel protein interaction dynamics within the tumour microenvironment.
ER  -

SINGH, Ashita; Monikaben PADARIYA; Jakub FAKTOR; Sachin KOTE; Sara MIKAC; Alicja DZIADOSZ; Tak W LAM; Jack BRYDON; Martin A WEAR; Kathryn L BALL; Ted HUPP; Alicja SZNARKOWSKA; Borek VOJTESEK a Umesh KALATHIYA. Identification of novel interferon responsive protein partners of human leukocyte antigen A (HLA-A) using cross-linking mass spectrometry (CLMS) approach. \textit{Scientific Reports}. Nature Research, 2022, roč.~12, č.~1, s.~1-16. ISSN~2045-2322. Dostupné z: https://doi.org/10.1038/s41598-022-21393-z.

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