China
Africa
Explore chapters and articles related to this topic
Family Caulimoviridae
Published in Paul Pumpens, Peter Pushko, Philippe Le Mercier, Virus-Like Particles, 2022
Paul Pumpens, Peter Pushko, Philippe Le Mercier
The virion-associated proteins (VAPs) are incorporated into the virion as a triskelion structure that cements three hexavalent or pentavalent capsomers together. The N-terminus of the VAP is facing out of the CaMV capsid. It contains two coiled-coil motifs with opposite handedness, forming dimers by antiparallel interaction with adjacent capsid molecules to create a network around the virus particle (Plisson et al. 2005). The VAP facilitates interaction of the virion with host and other viral proteins—i.e., the movement protein (MP) and the aphid transmission factor (ATF)—but is not essential for the virion formation.
Energy Demand of Muscle Machines
Published in Peter W. Hochachka, Muscles as Molecular and Metabolic Machines, 2019
Myosin is a very large molecule (500 kDa). It contains two identical major chains (200 kDa each) and four light chains (about 20 kDa each). Electron micrographs show that myosin consists of a double-headed globular region joined to a very long rod. The rod is a two-stranded α-helical coiled coil.
Integrin Receptors and Epiligrin in Cell-Cell and Cell-Substrate Adhesion in the Epidermis
Published in Yoshikazu Takada, Integrins: The Biological Problems, 2017
William G. Carter, Susana G. Gil, Banu E. Symington, Tod A. Brown, Shunji Hattori, Maureen C. Ryan
We have identified and sequenced multiple cDNA clones encoding the 170-kDa subunit of epiligrin (E170). Consistent with the immunological data above, partial sequence analysis of the cDNA clones for E170 revealed a correlation with domains IIIa and II of human laminin A chain. Domain IIIa encodes a cysteine-rich region containing EGF-like repeats.124C Sequence alignment of E170 and human laminin A chain in domain IIIa showed conservation of the cysteine residues and 55% sequence homology. In contrast to domain III, the primary amino acid sequence in domain II is not as well conserved between E170 and laminin A chain. However, a structural relationship is maintained in that both proteins encode alpha-helical domains characteristic of a coiled-coil structure previously described for laminin.123,124C Complete sequence analysis will be necessary to determine how E170 relates to the other domains present in the laminin A chain and to determine if E170 is derived from the same gene as one of the EE-laminin subunits.
Affinity-controlled capture and release of engineered monoclonal antibodies by macroporous dextran hydrogels using coiled-coil interactions
Published in mAbs, 2023
Seyed Farzad Baniahmad, Romane Oliverio, Ines Obregon-Gomez, Alma Robert, Anne E.G. Lenferink, Elena Pazos, Nick Virgilio, Xavier Banquy, Gregory De Crescenzo, Yves Durocher
Affinity peptides are versatile tunable tools that can be easily expressed as tags on recombinant proteins. This strategy ensures the efficient tagging of the protein since no extra conjugation step is required and removes the need for an additional purification step. Coiled-coil peptides are commonly used affinity systems derived from the coiled-coil structure, which is one of the most abundant naturally occurring motifs for protein folding and assembly.17 Structurally, this oligomerization motif consists of two or more α helices wrapped around each other. It is commonly found in many proteins involved in cellular activities, including transcription, muscle contractions, or viral fusion mechanisms.23–25 The fingerprint of this structure is a repeat of a seven-residue motif (heptad), the number of which can vary from 200 in naturally occurring fibrous proteins to only two heptads in a de novo designed synthetic coiled-coil.26 The E/K coiled coil is a de-novo-designed coiled-coil in which the Ecoil and Kcoil peptides, heptads: EVSALKE (Ecoil) and KVSALEK (Kcoil), form a highly specific, heterodimeric coiled-coil interaction with a high affinity, shown to be sufficiently strong in physiological conditions.27,28
Self-assembling peptides-based nano-cargos for targeted chemotherapy and immunotherapy of tumors: recent developments, challenges, and future perspectives
Published in Drug Delivery, 2022
Xue-Jun Wang, Jian Cheng, Le-Yi Zhang, Jun-Gang Zhang
Peptides can self-assemble into a variety of nanostructures in an aqueous solution under a variety of environmental conditions (Chen & Rosi, 2010). For example, when peptides are dissolved in a low-pH and high-osmotic pressure solution, nanofibers form rapidly. To rationally design objective structures, it is therefore beneficial to understand the structures of SAPs and the mechanism of SA (Zhao et al., 2019). Certain SAP structures have been reported to be stable, which makes them suitable for biological applications. For example, the coiled-coil structure is more stable than other ɑ-helices (Rad-Malekshahi et al., 2016). Numerous SAPs structures have a variety of bioapplications. According to studies, the structure of nanomaterials can affect the recognition and uptake of cells, as well as the immune response (Branco et al., 2011). When compared to hydrogels and β-sheet fibrils formed by peptides, nanofibers potentially facilitate the attachment, differentiation, and growth of different types of mammalian primary cells. Similarly, the fibrillated peptides can effectively enhance the responses of the antibodies, thus resulting in the production of specific antibodies without supplying any immune adjuvants (Davis et al., 2005; Yang et al., 2020b).
Isolation of monoclonal antibodies from anti-synthetase syndrome patients and affinity maturation by recombination of independent somatic variants
Published in mAbs, 2020
Luke Burman, Yeeting E. Chong, Sherie Duncan, Anders Klaus, Kaitlyn Rauch, Kristina Hamel, Karine Hervé, Stephanie Pfaffen, David W. Collins, Kevin Heyries, Leslie Nangle, Carl Hansen, David J. King
Histidyl-tRNA synthetase (HARS) is one of a number of aminoacyl-tRNA synthetases that have additional functions outside of protein synthesis, with both intracellular and extracellular non-canonical functions reported.22–25 Several aminoacyl-tRNA synthetases, including HARS as well as splice variants from their genes, are secreted and have potentially important roles in regulation of the immune system.26–29 Monoclonal antibodies to HARS are, therefore, of interest for their potential ability to regulate the immune system. The rare human autoimmune disease, Jo-1 positive anti-synthetase syndrome (ASS), is characterized by the presence of autoantibodies to HARS.30 These autoantibodies remove free HARS from the circulation and are associated with individuals exhibiting activated immune pathology.29 The HARS protein can be divided into three domains: 1) an N-terminal coiled-coil WHEP domain, 2) a central catalytic domain, and 3) a C-terminal anticodon binding domain (ABD). Autoantibodies have been reported to most frequently recognize epitopes within the N- or C-terminal domains.26 In this study, we set out to isolate human monoclonal antibodies to HARS from Jo-1 positive individuals, and to investigate the generation of high-affinity antibodies using the information available in related sequences.