Dengue and the Lectin Pathway of the Complement System

Autor: Panisadee Avirutnan, John P. Atkinson, M. Kathryn Liszewski, Nuntaya Punyadee, Romchat Kraivong
Jazyk: angličtina
Rok vydání: 2021
Předmět:
0301 basic medicine
viruses
lectin complement pathway
chemical and pharmacologic phenomena
dengue hemorrhagic fever
Review
Viral Nonstructural Proteins
Dengue virus
Biology
medicine.disease_cause
Mannose-Binding Lectin
Polymorphism
Single Nucleotide
Microbiology
Dengue fever
Dengue
03 medical and health sciences
0302 clinical medicine
flavivirus
Polysaccharides
Virology
medicine
Animals
Humans
dengue fever
Severe Dengue
Opsonin
Immune Evasion
Mannan-binding lectin
nonstructural protein NS1
dengue shock syndrome
Virulence
dengue virus
Pattern recognition receptor
Complement Pathway
Mannose-Binding Lectin
medicine.disease
biology.organism_classification
QR1-502
Complement system
Flavivirus
030104 developmental biology
Infectious Diseases
Receptors
Pattern Recognition
Lectin pathway
030215 immunology
Zdroj: Viruses, Vol 13, Iss 1219, p 1219 (2021)
Viruses
ISSN: 1999-4915
Popis: Dengue is a mosquito-borne viral disease causing significant health and economic burdens globally. The dengue virus (DENV) comprises four serotypes (DENV1-4). Usually, the primary infection is asymptomatic or causes mild dengue fever (DF), while secondary infections with a different serotype increase the risk of severe dengue disease (dengue hemorrhagic fever, DHF). Complement system activation induces inflammation and tissue injury, contributing to disease pathogenesis. However, in asymptomatic or primary infections, protective immunity largely results from the complement system’s lectin pathway (LP), which is activated through foreign glycan recognition. Differences in N-glycans displayed on the DENV envelope membrane influence the lectin pattern recognition receptor (PRR) binding efficiency. The important PRR, mannan binding lectin (MBL), mediates DENV neutralization through (1) a complement activation-independent mechanism via direct MBL glycan recognition, thereby inhibiting DENV attachment to host target cells, or (2) a complement activation-dependent mechanism following the attachment of complement opsonins C3b and C4b to virion surfaces. The serum concentrations of lectin PRRs and their polymorphisms influence these LP activities. Conversely, to escape the LP attack and enhance the infectivity, DENV utilizes the secreted form of nonstructural protein 1 (sNS1) to counteract the MBL effects, thereby increasing viral survival and dissemination.
Databáze: OpenAIRE
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