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10.1007/s12250-019-00190-5

http://scihub22266oqcxt.onion/10.1007/s12250-019-00190-5
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31916022!7035235!31916022
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suck abstract from ncbi

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  • Cryo-EM Studies of Virus-Antibody Immune Complexes #MMPMID31916022
  • Li N; Li Z; Fu Y; Cao S
  • Virol Sin 2020[Feb]; 35 (1): 1-13 PMID31916022show ga
  • Antibodies play critical roles in neutralizing viral infections and are increasingly used as therapeutic drugs and diagnostic tools. Structural studies on virus-antibody immune complexes are important for better understanding the molecular mechanisms of antibody-mediated neutralization and also provide valuable information for structure-based vaccine design. Cryo-electron microscopy (cryo-EM) has recently matured as a powerful structural technique for studying bio-macromolecular complexes. When combined with X-ray crystallography, cryo-EM provides a routine approach for structurally characterizing the immune complexes formed between icosahedral viruses and their antibodies. In this review, recent advances in the structural understanding of virus-antibody interactions are outlined for whole virions with icosahedral T = pseudo 3 (picornaviruses) and T = 3 (flaviviruses) architectures, focusing on the dynamic nature of viral shells in different functional states. Glycoprotein complexes from pleomorphic enveloped viruses are also discussed as immune complex antigens. Improving our understanding of viral epitope structures using virus-based platforms would provide a fundamental road map for future vaccine development.
  • |*Cryoelectron Microscopy[MESH]
  • |Animals[MESH]
  • |Antibodies, Viral/immunology/*ultrastructure[MESH]
  • |Antigen-Antibody Complex/*ultrastructure[MESH]
  • |Epitopes/immunology/ultrastructure[MESH]
  • |Flavivirus/immunology/ultrastructure[MESH]
  • |Humans[MESH]
  • |Picornaviridae/immunology/ultrastructure[MESH]
  • |Protein Binding[MESH]
  • |Protein Conformation[MESH]
  • |Virion/immunology/*ultrastructure[MESH]


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  • suck abstract from ncbi

    1 1.35 2020