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Effects of MASP 2 haplotypes and MASP ‐2 levels in hepatitis C‐infected patients
Author(s) -
Silva Amanda A.,
Catarino Sandra J.,
Boldt Angelica B. W.,
Pedroso Maria Lucia A.,
Beltrame Marcia H.,
MessiasReason Iara J.
Publication year - 2018
Publication title -
international journal of immunogenetics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.41
H-Index - 47
eISSN - 1744-313X
pISSN - 1744-3121
DOI - 10.1111/iji.12371
Subject(s) - haplotype , genotype , immunology , lectin pathway , hepatitis c , mannan binding lectin , biology , medicine , virology , complement system , gene , antibody , lectin , genetics , alternative complement pathway
Summary Mannan‐binding lectin ( MBL ) and MBL ‐associated serine protease 2 ( MASP ‐2) are components of the lectin pathway, which activate the complement system after binding to the HCV structural proteins E1 and E2. We haplotyped 11 MASP 2 polymorphisms in 103 HCV patients and 205 controls and measured MASP ‐2 levels in 67 HCV patients and 77 controls to better understand the role of MASP ‐2 in hepatitis C susceptibility and disease severity according to viral genotype and fibrosis levels. The haplotype block MASP 2* ARDP was associated with protection against HCV infection ( OR = 0.49, p = .044) and lower MASP ‐2 levels in controls ( p = .021), while haplotype block AGTDVRC was significantly increased in patients ( OR = 7.58, p = .003). MASP ‐2 levels were lower in patients than in controls ( p < .001) and in patients with viral genotype 1 or 4 (poor responders to treatment) than genotype 3 ( p = .022) and correlated inversely with the levels of alkaline phosphatase, especially in individuals with fibrosis 3 or 4 ( R = −.7, p = .005). MASP 2 gene polymorphisms modulate basal gene expression, which may influence the quality of complement response against HCV . MASP ‐2 levels decrease during chronic disease, independently of MASP 2 genotypes, most probably due to consumption and attenuation mechanisms of viral origin and by the reduced liver function, the site of MASP ‐2 production.