Results 61 to 70 of about 5,389 (128)

Structure of the human astrovirus capsid spike in complex with the neonatal Fc receptor

Nature Communications
Human astroviruses (HAstVs) are a leading cause of viral gastroenteritis in children worldwide. Recently the neonatal Fc receptor (FcRn) was identified as a receptor for HAstV, however the molecular basis for the FcRn-HAstV interaction remained unclear ...
Adam Lentz, Sarah Lanning, Khurshid R. Iranpur, Lena Ricemeyer, Carlos F. Arias, Rebecca M. DuBois   +5 more
doaj   +1 more source

FcRn-enhancing mutations lead to increased and prolonged levels of the HIV CCR5-blocking monoclonal antibody leronlimab in the fetuses and newborns of pregnant rhesus macaques

mAbs
Prenatal administration of monoclonal antibodies (mAbs) is a strategy that could be exploited to prevent viral infections during pregnancy and early life.
Joanna Zikos, Gabriela M. Webb, Helen L. Wu, Jason S. Reed, Jennifer Watanabe, Jodie L. Usachenko, Ala M. Shaqra, Celia A. Schiffer, Koen K. A. Van Rompay, Jonah B. Sacha, Diogo M. Magnani   +10 more
doaj   +1 more source

Mutations of Recombinant Aquaporin-4 Antibody in the Fc Domain Can Impair Complement-Dependent Cellular Cytotoxicity and Transplacental Transport

Frontiers in Immunology, 2018
Maternal antibodies provide protection for the developing fetus. Transplacental transport of pathogenic autoantibodies might pose a risk for the developing fetus. The transport of antibodies across the placenta to the fetal circulation occurs through the
Simone Mader, Lior Brimberg, John N. Soltys, Jeffrey L. Bennett, Jeffrey L. Bennett, Betty Diamond   +5 more
doaj   +1 more source

Unraveling the interaction between FcRn and albumin: opportunities for design of albumin-based therapeutics

Frontiers in Immunology, 2015
The neonatal Fc receptor (FcRn) was first found to be responsible for transporting antibodies of the immunoglobulin G (IgG) class from the mother to the fetus or neonate as well as for protecting IgG from intracellular catabolism.
Kine Marita Knudsen Sand, Kine Marita Knudsen Sand, Malin eBern, Malin eBern, Jeannette eNilsen, Jeannette eNilsen, Hanna Theodora eNoordzij, Hanna Theodora eNoordzij, Inger eSandlie, Inger eSandlie, Jan Terje eAndersen   +10 more
doaj   +1 more source

Engineering FcRn binding kinetics dramatically extends antibody serum half-life and enhances therapeutic potential

Journal of Biological Engineering
Background Optimizing the IgG Fc domain for neonatal Fc receptor (FcRn) binding is crucial for enhancing antibody pharmacokinetics. The prolonged serum half-life of IgG antibody is governed by its pH-dependent interaction with FcRn, enabling efficient ...
Sanghwan Ko, Migyeong Jo, Munsu Kyung, Wonju Lee, Woo Hyung Ko, Jung-Hyun Na, Youn Seo Chun, Byoung Joon Ko, Sang Taek Jung   +8 more
doaj   +1 more source

Fully human monoclonal antibody inhibitors of the neonatal Fc receptor (FcRn) reduce circulating IgG in nonhuman primates

Frontiers in Immunology, 2015
The therapeutic management of antibody mediated autoimmune disease typically involves immunosuppressant and immunomodulatory strategies. However, perturbing the fundamental role of the neonatal Fc receptor (FcRn) in salvaging IgG from lysosomal ...
Andrew E Nixon, Jie eChen, Daniel J Sexton, Arumugam eMuruganandam, Alan J Bitonti, Jennifer eDumont, Malini eViswanathan, Diana eMartik, Dina eWassaf, Adam eMezo, Clive R Wood, Joseph C Biedenkapp, Christopher eTenHoor   +12 more
doaj   +1 more source

Binding to the neonatal Fc receptor enhances the pathogenicity of anti-desmoglein-3 antibodies in keratinocytes

Frontiers in Immunology
The neonatal Fc receptor (FcRn) is important for numerous cellular processes that involve antibody recycling and trafficking. A major function of FcRn is IgG recycling and half-life prolongation, and FcRn blockade results in a reduction of autoantibodies
Anna Zakrzewicz, Katrien Vanderheyden, Yad Galaly, Simon Feldhoff, Magdalena Sips, Maximilian Brinkhaus, Ritva Tikkanen   +6 more
doaj   +1 more source

Antibody Fc engineering for enhanced neonatal Fc receptor binding and prolonged circulation half-life

mAbs, 2019
The neonatal Fc receptor (FcRn) promotes antibody recycling through rescue from normal lysosomal degradation. The binding interaction is pH-dependent with high affinity at low pH, but not under physiological pH conditions.
Brian C. Mackness, Julie A. Jaworski, Ekaterina Boudanova, Anna Park, Delphine Valente, Christine Mauriac, Olivier Pasquier, Thorsten Schmidt, Mostafa Kabiri, Abdullah Kandira, Katarina Radošević, Huawei Qiu   +11 more
doaj   +1 more source

Advanced human FcRn knock-in mice for pharmacokinetic profiling of therapeutic antibodies

Scientific Reports
IgG-based therapeutic antibodies are increasingly adopted for diverse human diseases, such as cancer and autoimmune disorders displaying remarkable therapeutic performance.
SuBin Lee, Munsu Kyung, Miyeon Park, Sunha Park, JaeHoon Lee, Suyeon Kim, Seunghyeon Lee, Migyeong Jo, Sang Taek Jung, Han-Woong Lee   +9 more
doaj   +1 more source

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

mAbs
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, Jan Terje Andersen, Ulrich Rant, Tilman Schlothauer   +3 more
doaj   +1 more source