Results 21 to 30 of about 10,163 (201)

The neonatal Fc receptor (FcRn) is a pan-arterivirus receptor

open access: yesNature Communications
Arteriviruses infect a variety of mammalian hosts, but the receptors used by these viruses to enter cells are poorly understood. We identified the neonatal Fc receptor (FcRn) as an important pro-viral host factor via comparative genome-wide CRISPR ...
Teressa M. Shaw   +15 more
doaj   +2 more sources

Functional characterization of DPP4 and FcRn as receptor and coreceptor for classical human astroviruses in Caco-2 cells.

open access: yesPLoS Pathogens
Classical human astroviruses (HAstV) are a global cause of viral gastroenteritis, particularly in children and immunocompromised individuals. Despite their clinical significance, the biology of HAstV remains poorly understood.
Catalina Aguilera-Flores   +8 more
doaj   +2 more sources

Insight into the avidity–affinity relationship of the bivalent, pH-dependent interaction between IgG and FcRn

open access: yesmAbs
Monoclonal antibodies (mAbs) as therapeutics necessitate favorable pharmacokinetic properties, including extended serum half-life, achieved through pH-dependent binding to the neonatal Fc receptor (FcRn).
Johannes Reusch   +3 more
doaj   +2 more sources

FcRn regulates antigen presentation in dendritic cells downstream of DEC205-targeted vaccines

open access: yesnpj Vaccines
Dendritic cell (DC)-targeted vaccination is a new mode of antigen delivery that relies on the use of monoclonal antibodies (mAb) to target antigen to specific DC subsets.
Christophe Macri   +9 more
doaj   +2 more sources

The neonatal Fc receptor (FcRn) is required for porcine reproductive and respiratory syndrome virus uncoating

open access: yesJournal of Virology
Porcine reproductive and respiratory syndrome virus (PRRSV) continues to cause substantial economic losses to the pig industry worldwide. Previous studies from other groups showed that CD163 is required for PRRSV uncoating and genome release.
Kang Yang   +7 more
doaj   +2 more sources

FcRn-guided antigen trafficking enhances cancer vaccine efficacy

open access: yesCancer Immunology, Immunotherapy
The development of tumor vaccines represents a significant focus within cancer therapeutics research. Nonetheless, the efficiency of antigen presentation in tumor vaccine remains suboptimal.
Mengyu Hong   +16 more
doaj   +3 more sources

In Translation: FcRn across the Therapeutic Spectrum [PDF]

open access: yesInternational Journal of Molecular Sciences, 2021
As an essential modulator of IgG disposition, the neonatal Fc receptor (FcRn) governs the pharmacokinetics and functions many therapeutic modalities. In this review, we thoroughly reexamine the hitherto elucidated biological and thermodynamic properties of FcRn to provide context for our assessment of more recent advances, which covers antigen-binding ...
Timothy Qi, Yanguang Cao
openaire   +2 more sources

Distribution of FcRn Across Species and Tissues [PDF]

open access: yesJournal of Histochemistry & Cytochemistry, 2017
The neonatal Fc receptor (FcRn) is a major histocompatibility complex class I type molecule that binds to, transports, and recycles immunoglobulin G (IgG) and albumin, thereby protecting them from lysosomal degradation. Therefore, besides the knowledge of FcRn affinity, FcRn protein expression is critical in understanding the pharmacokinetic behavior ...
Sari, Latvala   +4 more
openaire   +4 more sources

The Role of FcRn in Antigen Presentation [PDF]

open access: yesFrontiers in Immunology, 2014
Immunoglobulins are unique molecules capable of simultaneously recognizing a diverse array of antigens and themselves being recognized by a broad array of receptors. The abundance specifically of the IgG subclass and the variety of signaling receptors to which it binds render this an important immunomodulatory molecule. In addition to the classical Fcγ
Kristi eBaker   +4 more
openaire   +4 more sources

Surmounting an Impasse of FcRn Structure [PDF]

open access: yesStructure, 2013
FcRn, resembling a major histocompatibility complex class I molecule with a closed peptide cleft, is an intracellular molecule that binds endocytosed albumin and IgG by a pH-dependent mechanism, diverting them from degradative fates and moving them out of the cell.
Anderson, Clark L., Kim, Jonghan
openaire   +2 more sources

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