Complement-Independent Modulation of Influenza A Virus Infection by Factor H.


Journal

Frontiers in immunology
ISSN: 1664-3224
Titre abrégé: Front Immunol
Pays: Switzerland
ID NLM: 101560960

Informations de publication

Date de publication:
2020
Historique:
received: 15 01 2020
accepted: 13 02 2020
entrez: 10 4 2020
pubmed: 10 4 2020
medline: 2 3 2021
Statut: epublish

Résumé

The complement system is an ancient innate immune defense mechanism that can recognize molecular patterns on the invading pathogens. Factor H, as an inhibitor of the alternative pathway, down-regulates complement activation on the host cell surface. Locally synthesized factor H at the site of infection/injury, including lungs, can act as a pattern recognition molecule without involving complement activation. Here, we report that factor H, a sialic acid binder, interacts with influenza A virus (IAV) and modulates IAV entry, as evident from down-regulation of matrix protein 1 (M1) in H1N1 subtype-infected cells and up-regulation of M1 expression in H3N2-infected A549 cells. Far-western blot revealed that factor H binds hemagglutinin (HA, ~70 kDa), neuraminidase (NA, ~60 kDa), and M1 (~25 kDa). IAV-induced transcriptional levels of IFN-α, TNF-α, IL-12, IL-6, IFN-α, and RANTES were reduced following factor H treatment for the H1N1 subtype at 6 h post-infection. However, for the H3N2 subtype, mRNA levels of these pro-inflammatory cytokines were enhanced. A recombinant form of vaccinia virus complement control protein (VCP), which like factor H, contains CCP modules and has complement-regulatory activity, mirrored the results obtained with factor H. Both factor H (25%), and VCP (45%) were found to reduce luciferase reporter activity in MDCK cells transduced with H1N1 pseudotyped lentiviral particles. Factor H (50%) and VCP (30%) enhanced the luciferase reporter activity for H3N2, suggesting an entry inhibitory role of factor H and VCP against H1N1, but not H3N2. Thus, factor H can modulate IAV infection and inflammatory responses, independent of its complement-related functions.

Identifiants

pubmed: 32269562
doi: 10.3389/fimmu.2020.00355
pmc: PMC7109256
doi:

Substances chimiques

Anti-Inflammatory Agents 0
Complement Inactivating Agents 0
Complement Factor H 80295-65-4
Complement System Proteins 9007-36-7

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

355

Informations de copyright

Copyright © 2020 Murugaiah, Varghese, Saleh, Tsolaki, Alrokayan, Khan, Collison, Sim, Nal, Al-Mohanna and Kishore.

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Auteurs

Valarmathy Murugaiah (V)

Biosciences, College of Health and Life Sciences, Brunel University London, Uxbridge, United Kingdom.

Praveen M Varghese (PM)

Biosciences, College of Health and Life Sciences, Brunel University London, Uxbridge, United Kingdom.
School of Biosciences and Technology, Vellore Institute of Technology, Vellore, India.

Soad M Saleh (SM)

Department of Cell Biology, King Faisal Specialist Hospital and Research Centre, Riyadh, Saudi Arabia.

Anthony G Tsolaki (AG)

Biosciences, College of Health and Life Sciences, Brunel University London, Uxbridge, United Kingdom.

Salman H Alrokayan (SH)

Department of Biochemistry, College of Science, King Saud University, Riyadh, Saudi Arabia.

Haseeb A Khan (HA)

Department of Biochemistry, College of Science, King Saud University, Riyadh, Saudi Arabia.

Kate S Collison (KS)

Department of Cell Biology, King Faisal Specialist Hospital and Research Centre, Riyadh, Saudi Arabia.

Robert B Sim (RB)

Department of Biochemistry, University of Oxford, Oxford, United Kingdom.

Béatrice Nal (B)

Biosciences, College of Health and Life Sciences, Brunel University London, Uxbridge, United Kingdom.

Futwan A Al-Mohanna (FA)

Department of Cell Biology, King Faisal Specialist Hospital and Research Centre, Riyadh, Saudi Arabia.

Uday Kishore (U)

Biosciences, College of Health and Life Sciences, Brunel University London, Uxbridge, United Kingdom.

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Classifications MeSH