Heterogeneity of MBL–MASP complexes

Mayilyan, Karine R.; Presanis, Julia S.; Arnold, James N.; Hajela, Krishnan; Sim, Robert B.

doi:10.1016/j.molimm.2005.07.011

Cited by 27 publications

(22 citation statements)

References 35 publications

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“…This might reflect a lower level of MASP-2 synthesis (as suggest our preliminary data; Swierzko et al, unpublished data) and invites the hypothesis that in the first period of life, MBL acts mainly as an opsonin, whereas the lectin pathway activation has minor significance in innate immune defense. Because MASP-2 competes for binding to MBL with other MBLassociated serine proteases and MAp19 (itself a truncated form, being a product of alternative splicing of the MASP2 gene) [33,34], it might be speculated that the relatively low ability to cleave C4 results from a variable (dynamic) balance among MASPs during ontogenesis. The major conclusion from this study, by far the largest series of its kind, is that inferring serum MBL from genotype is unreliable for individuals and the use of this approach for disease cohorts has limited validity.…”

Section: Discussionmentioning

confidence: 99%

Mannan-binding lectin genotypes and genotype–phenotype relationships in a large cohort of Polish neonates

et al. 2009

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Section: Discussionmentioning

confidence: 99%

Mannan-binding lectin genotypes and genotype–phenotype relationships in a large cohort of Polish neonates

et al. 2009

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“…Plates were incubated for 1 h on ice. MBL/MASP-2 complex activity was assayed as previously described (Mayilyan et al, 2006) with modifications. Wells were washed twice at 37°C with 20 mM HEPES, 1 M NaCl, 5 mM CaCl 2 , 0.1% (v/v) Tween-20, pH 7.4 and twice with 20 mM HEPES, 140 mM NaCl, 5 mM CaCl 2 , pH 7.4 (wash buffer).…”

Section: Production Of Cell Culture Infectious Hcv (Hcvcc) and Neutramentioning

confidence: 99%

Specific interaction of hepatitis C virus glycoproteins with mannan binding lectin inhibits virus entry

et al. 2010

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Mannan-binding lectin (MBL) is a soluble innate immune protein that binds to glycosylated targets. MBL acts as an opsonin and activates complement, contributing to the destruction and clearance of infecting microorganisms. Hepatitis C virus (HCV) encodes two envelope glycoproteins E1 and E2, expressed as non-covalent E1/E2 heterodimers in the viral envelope. E1 and E2 are potential ligands for MBL. Here we describe an analysis of the interaction between HCV and MBL using recombinant soluble E2 ectodomain fragment, the full-length E1/E2 heterodimer, expressed in vitro, and assess the effect of this interaction on virus entry. A binding assay using antibody capture of full length E1/E2 heterodimers was used to demonstrate calcium dependent, saturating binding of MBL to HCV glycoproteins. Competition with various saccharides further confirmed that the interaction was via the lectin domain of MBL. MBL binds to E1/E2 representing a broad range of virus genotypes. MBL was shown to neutralize the entry into Huh-7 cells of HCV pseudoparticles (HCVpp) bearing E1/E2 from a wide range of genotypes. HCVpp were neutralized to varying degrees. MBL was also shown to neutralize an authentic cell culture infectious virus, strain JFH-1 (HCVcc). Furthermore, binding of MBL to E1/E2 was able to activate the complement system via MBL-associated serine protease 2. In conclusion, MBL interacts directly with HCV glycoproteins, which are present on the surface of the virion, resulting in neutralization of HCV particles.

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“…Exploration of L-ficolin-MASP complex activity showed that schizophrenic patients had more than 40% increase in serum L-ficolin level and 15% in L-ficolin-MASP-2 activity when compared with controls. 69 MBL-MASP complexes are heterogeneous, 77 in that MBL itself forms oligomers of different sizes, and each MBL oligomer may bind only one of MASP-1, -2 or -3. In individuals with high MBL concentration there may be excess free MBL not occupied by MASPs, particularly not by MASP-2.…”

Section: The Alternative and Lectin Pathways In Schizophreniamentioning

confidence: 99%