Complement cascade

The complement cascade is a biochemical process in the blood that helps or 'complements' cells of the immune system to eliminate invading pathogens. When activated by one of three pathways, a cascade of serial cleavage events results in a marked amplification of the immune response and formation of the cell-killing membrane attack complex.

Latest Research and Reviews

  • Reviews |

    This Review presents our current understanding of C3 glomerulopathy. Smith et al. discuss the histopathological diagnosis and the crucial pathogenic role of complement dysregulation. Genetic and acquired drivers of C3 glomerulopathy, potential biomarkers and available treatments are highlighted.

    • Richard J. H. Smith
    • , Gerald B. Appel
    • , Anna M. Blom
    • , H. Terence Cook
    • , Vivette D D’Agati
    • , Fadi Fakhouri
    • , Véronique Fremeaux-Bacchi
    • , Mihály Józsi
    • , David Kavanagh
    • , John D. Lambris
    • , Marina Noris
    • , Matthew C. Pickering
    • , Giuseppe Remuzzi
    • , Santiago Rodriguez de Córdoba
    • , Sanjeev Sethi
    • , Johan Van der Vlag
    • , Peter F. Zipfel
    •  & Carla M. Nester
  • Research |

    ApoE is a direct checkpoint inhibitor of unresolvable inflammation in neurodegenerative and cardiovascular diseases

    • Changjun Yin
    • , Susanne Ackermann
    • , Zhe Ma
    • , Sarajo K. Mohanta
    • , Chuankai Zhang
    • , Yuanfang Li
    • , Sandor Nietzsche
    • , Martin Westermann
    • , Li Peng
    • , Desheng Hu
    • , Sai Vineela Bontha
    • , Prasad Srikakulapu
    • , Michael Beer
    • , Remco T. A. Megens
    • , Sabine Steffens
    • , Markus Hildner
    • , Luke D. Halder
    • , Hans-Henning Eckstein
    • , Jaroslav Pelisek
    • , Jochen Herms
    • , Sigrun Roeber
    • , Thomas Arzberger
    • , Anna Borodovsky
    • , Livia Habenicht
    • , Christoph J. Binder
    • , Christian Weber
    • , Peter F. Zipfel
    • , Christine Skerka
    •  & Andreas J. R. Habenicht
  • Research | | open

    The complement membrane attack complex (MAC) is a lytic immune pore that kills pathogens. Here the authors use cryoEM to provide a structural and biophysical mechanism for how β-pore forming proteins breach the lipid bilayer, providing pathways to explore pore-formation in molecular detail.

    • Anaïs Menny
    • , Marina Serna
    • , Courtney M. Boyd
    • , Scott Gardner
    • , Agnel Praveen Joseph
    • , B. Paul Morgan
    • , Maya Topf
    • , Nicholas J. Brooks
    •  & Doryen Bubeck
  • Research | | open

    Zika virus infection can cause severe disease in humans and there are currently no specific treatments or vaccines. Here, Bailey et al. isolate antibodies recognizing non-structural protein NS1 and show that they protect mice from disease by an Fc-dependent, non-neutralizing mechanism.

    • Mark J. Bailey
    • , James Duehr
    • , Harrison Dulin
    • , Felix Broecker
    • , Julia A. Brown
    • , Fortuna O. Arumemi
    • , Maria C. Bermúdez González
    • , Victor H. Leyva-Grado
    • , Matthew J. Evans
    • , Viviana Simon
    • , Jean K. Lim
    • , Florian Krammer
    • , Rong Hai
    • , Peter Palese
    •  & Gene S. Tan
  • Research | | open

    Complement, while serving to remove pathogens in the circulation, is also important for synergizing with inflammasomes to modulate CD4 T cell activation. Here the authors show that CD46, a complement receptor expressed only in humans, is essential for inducing optimal activation and effector functions of human CD8 T cells.

    • Giuseppina Arbore
    • , Erin E. West
    • , Jubayer Rahman
    • , Gaelle Le Friec
    • , Nathalie Niyonzima
    • , Mehdi Pirooznia
    • , Ilker Tunc
    • , Polychronis Pavlidis
    • , Nicholas Powell
    • , Yuesheng Li
    • , Poching Liu
    • , Aude Servais
    • , Lionel Couzi
    • , Veronique Fremeaux-Bacchi
    • , Leo Placais
    • , Alastair Ferraro
    • , Patrick R. Walsh
    • , David Kavanagh
    • , Behdad Afzali
    • , Paul Lavender
    • , Helen J. Lachmann
    •  & Claudia Kemper
  • Research | | open

    The Complement component 9 (C9) is the pore-forming component of the Membrane Attack Complex which targets pathogens. Here authors use structural biology to compare monomeric C9 to C9 within the polymeric assembly and identify the element which inhibits C9 self-assembly in the absence of the target membrane.

    • Bradley A. Spicer
    • , Ruby H. P. Law
    • , Tom T. Caradoc-Davies
    • , Sue M. Ekkel
    • , Charles Bayly-Jones
    • , Siew-Siew Pang
    • , Paul J. Conroy
    • , Georg Ramm
    • , Mazdak Radjainia
    • , Hariprasad Venugopal
    • , James C. Whisstock
    •  & Michelle A. Dunstone

News and Comment