Biochemical evidence for conformational variants in the anti-viral and pro-metastatic protein IFITM1

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00209805%3A_____%2F24%3A00079658" target="_blank" >RIV/00209805:_____/24:00079658 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/00216224:14310/24:00136749

Výsledek na webu

<a href="https://pubmed.ncbi.nlm.nih.gov/38379409/" target="_blank" >https://pubmed.ncbi.nlm.nih.gov/38379409/</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1515/hsz-2023-0327" target="_blank" >10.1515/hsz-2023-0327</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Biochemical evidence for conformational variants in the anti-viral and pro-metastatic protein IFITM1

Popis výsledku v původním jazyce

Interferon induced transmembrane proteins (IFITMs) play a dual role in the restriction of RNA viruses and in cancer progression, yet the mechanism of their action remains unknown. Currently, there is no data about the basic biochemical features or biophysical properties of the IFITM1 protein. In this work, we report on description and biochemical characterization of three conformational variants/oligomeric species of recombinant IFITM1 protein derived from an Escherichia coli expression system. The protein was extracted from the membrane fraction, affinity purified, and separated by size exclusion chromatography where two distinct oligomeric species were observed in addition to the expected monomer. These species remained stable upon re-chromatography and were designated as &quot;dimer&quot; and &quot;oligomer&quot; according to their estimated molecular weight. The dimer was found to be less stable compared to the oligomer using circular dichroism thermal denaturation and incubation with a reducing agent. A two-site ELISA and HDX mass spectrometry suggested the existence of structural motif within the N-terminal part of IFITM1 which might be significant in oligomer formation. Together, these data show the unusual propensity of recombinant IFITM1 to naturally assemble into very stable oligomeric species whose study might shed light on IFITM1 anti-viral and pro-oncogenic functions in cells.

Název v anglickém jazyce

Biochemical evidence for conformational variants in the anti-viral and pro-metastatic protein IFITM1

Popis výsledku anglicky

Interferon induced transmembrane proteins (IFITMs) play a dual role in the restriction of RNA viruses and in cancer progression, yet the mechanism of their action remains unknown. Currently, there is no data about the basic biochemical features or biophysical properties of the IFITM1 protein. In this work, we report on description and biochemical characterization of three conformational variants/oligomeric species of recombinant IFITM1 protein derived from an Escherichia coli expression system. The protein was extracted from the membrane fraction, affinity purified, and separated by size exclusion chromatography where two distinct oligomeric species were observed in addition to the expected monomer. These species remained stable upon re-chromatography and were designated as &quot;dimer&quot; and &quot;oligomer&quot; according to their estimated molecular weight. The dimer was found to be less stable compared to the oligomer using circular dichroism thermal denaturation and incubation with a reducing agent. A two-site ELISA and HDX mass spectrometry suggested the existence of structural motif within the N-terminal part of IFITM1 which might be significant in oligomer formation. Together, these data show the unusual propensity of recombinant IFITM1 to naturally assemble into very stable oligomeric species whose study might shed light on IFITM1 anti-viral and pro-oncogenic functions in cells.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

<a href="/cs/project/GA22-02940S" target="_blank" >GA22-02940S: Regulace signální dráhy IFN-γ pomocí inhibitorů HSP90</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2024

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Biological chemistry

ISSN

1431-6730

e-ISSN

1437-4315

Svazek periodika

405

Číslo periodika v rámci svazku

5

Stát vydavatele periodika

DE - Spolková republika Německo

Počet stran výsledku

14

Strana od-do

311-324

Kód UT WoS článku

001173488600001

EID výsledku v databázi Scopus

2-s2.0-85185789619