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001-es BibID:	BIBFORM104263
035-os BibID:	(cikkazonosító)999233 (Scopus)85141175162 (WOS)000888173300001 (PubMed)36341352
Első szerző:	Miltner Noémi (molekuláris biológus)
Cím:	Early suppression of antiviral host response and protocadherins by SARS-CoV-2 Spike protein in THP-1-derived macrophage-like cells / Miltner Noémi, Linkner Tamás Richárd, Ambrus Viktor, Al-Muffti Aya S., Ahmad Hala, Mótyán János András, Benkő Szilvia, Tőzsér József, Mahdi Mohamed
Dátum:	2022
ISSN:	1664-3224
Megjegyzések:	The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is the causative agent of coronavirus disease-19 (COVID-19). The spike protein (S) of SARS-CoV-2 plays a crucial role in mediating viral infectivity; hence, in an extensive effort to curb the pandemic, many urgently approved vaccines rely on the expression of the S protein, aiming to induce a humoral and cellular response to protect against the infection. Given the very limited information about the effects of intracellular expression of the S protein in host cells, we aimed to characterize the early cellular transcriptomic changes induced by expression of the S protein in THP-1-derived macrophage-like cells. Results showed that a wide variety of genes were differentially expressed, products of which are mainly involved in cell adhesion, homeostasis, and most notably, antiviral and immune responses, depicted by significant downregulation of protocadherins and type I alpha interferons (IFNAs). While initially, the levels of IFNAs were higher in the medium of S protein expressing cells, the downregulation observed on the transcriptomic level might have been reflected by no further increase of IFNA cytokines beyond the 5 h time-point, compared to the mock control. Our study highlights the intrinsic pathogenic role of the S protein and sheds some light on the potential drawbacks of its utilization in the context of vaccination strategies.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk SARS-CoV-2 coronavirus COVID-19 spike protein transcriptomics virology
Megjelenés:	Frontiers in Immunology. - 13 (2022), p. 999233. -
További szerzők:	Linkner Tamás Richárd Ambrus Viktor Attila (1989-) (biotechnológus) Al-Muffti, Aya S. Ahmad, Hala Mótyán János András (1981-) (biokémikus, molekuláris biológus) Benkő Szilvia (1973-) (molekuláris biológus) Tőzsér József (1959-) (molekuláris biológus, biokémikus, vegyész) Mahdi, Mohamed (1979-) (orvos, tudományos segédmunkatárs)
Pályázati támogatás:	TKP2021-EGA-20 Egyéb POST-COVID2021-16 Egyéb K131844 OTKA
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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001-es BibID:	BIBFORM050899
035-os BibID:	PMID:24044430 Article ID: 275
Első szerző:	Mótyán János András (biokémikus, molekuláris biológus)
Cím:	A molecular model of the full-length human NOD-like receptor family CARD domain containing 5 (NLRC5) protein / János András Mótyán, Péter Bagossi, Szilvia Benkő, József Tőzsér
Dátum:	2013
ISSN:	1471-2105
Megjegyzések:	Pattern recognition receptors of the immune system have key roles in the regulation of pathways after the recognition of microbial- and danger-associated molecular patterns in vertebrates. Members of NOD-like receptor (NLR) family typically function intracellularly. The NOD-like receptor family CARD domain containing 5 (NLRC5) is the largest member of this family that also contains the largest number of leucine-rich repeats (LRRs).Due to the lack of crystal structures of full-length NLRs, projects have been initiated with the aim to model certain or all members of the family, but systematic studies did not model the full-length NLRC5 due to its unique domain architecture.Our aim was to analyze the LRR sequences of NLRC5 and some NLRC5-related proteins and to build a model for the full-length human NLRC5 by homology modeling. RESULTS: LRR sequences of NLRC5 were aligned and were compared with the consensus pattern of ribonuclease inhibitor protein (RI)-like LRR subfamily. Two types of alternating consensus patterns previously identified for RI repeats were also found in NLRC5. A homology model for full-length human NLRC5 was prepared and, besides the closed conformation of monomeric NLRC5, a heptameric platform was also modeled for the opened conformational NLRC5 monomers. CONCLUSIONS: Identification of consensus patterns of leucine-rich repeat sequences helped to identify LRRs in NLRC5 and to predict their number and position within the protein. In spite of the lack of fully adequate template structures, the presence of an untypical CARD domain and unusually high number of LRRs in NLRC5, we were able to construct a homology model for both the monomeric and homo-heptameric full-length human NLRC5 protein.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban NLRC5 Molecular modeling LRR protein NOD-like receptor
Megjelenés:	BMC Bioinformatics 14 : 1 (2013), p. 1-11. -
További szerzők:	Bagossi Péter (1966-2011) (biokémikus, vegyész) Benkő Szilvia (1973-) (molekuláris biológus) Tőzsér József (1959-) (molekuláris biológus, biokémikus, vegyész)
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