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Udgivet

The lectin pathway of complement: advantage or disadvantage in HIV pathogenesis?

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

DOI

  1. Pre-transplant levels of ficolin-3 are associated with kidney graft survival

    Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

  2. Adjuvanted HLA-supertype restricted subdominant peptides induce new T-cell immunity during untreated HIV-1-infection

    Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

  1. Complement activation is a crucial driver of acute kidney injury in rhabdomyolysis

    Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

  2. Hyperbaric oxygen treatment is associated with a decrease in cytokine levels in patients with necrotizing soft-tissue infection

    Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

  3. Identification of two different coagulation phenotypes in people living with HIV with undetectable viral replication

    Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

  4. Hepatic steatosis associated with exposure to elvitegravir and raltegravir

    Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

Vis graf over relationer

The pattern recognition molecules of the lectin complement pathway are important components of the innate immune system with known functions in host-virus interactions. This paper summarizes current knowledge of how these intriguing molecules, including mannose-binding lectin (MBL), Ficolin-1, -2 and -3, and collectin-11 (CL-11) may influence HIV-pathogenesis. It has been demonstrated that MBL is capable of binding and neutralizing HIV and may affect host susceptibility to HIV infection and disease progression. In addition, MBL may cause variations in the host immune response against HIV. Ficolin-1, -2 and -3 and CL-11 could have similar functions in HIV infection as the ficolins have been shown to play a role in other viral infections, and CL-11 resembles MBL and the ficolins in structure and binding capacity.

OriginalsprogEngelsk
TidsskriftClinical immunology (Orlando, Fla.)
Vol/bind154
Udgave nummer1
Sider (fra-til)13-25
Antal sider13
ISSN1521-6616
DOI
StatusUdgivet - sep. 2014

ID: 44728942