scholarly journals Mannose-Binding Lectin Binds to a Range of Clinically Relevant Microorganisms and Promotes Complement Deposition

2000 ◽  
Vol 68 (2) ◽  
pp. 688-693 ◽  
Author(s):  
Olaf Neth ◽  
Dominic L. Jack ◽  
Alister W. Dodds ◽  
Helen Holzel ◽  
Nigel J. Klein ◽  
...  
Keyword(s):  
Immune Defense ◽  
Mannose Binding Lectin ◽  
Dependent Manner ◽  
Group B Streptococci ◽  
Concentration Dependent Manner ◽  
Mannose Binding ◽  
Low Levels ◽  
Serum Lectin ◽  
Group B ◽  
Binding Lectin

ABSTRACT Mannose-binding lectin (MBL) is a collagenous serum lectin believed to be of importance in innate immunity. Genetically determined low levels of the protein are known to predispose to infections. In this study the binding of purified MBL to pathogens isolated from immunocompromised children was investigated by flow cytometry. DiverseCandida species, Aspergillus fumigatus,Staphylococcus aureus, and beta-hemolytic group A streptococci exhibited strong binding of MBL, whereas Escherichia coli, Klebsiella species, and Haemophilus influenzae type b were characterized by heterogeneous binding patterns. In contrast, beta-hemolytic group B streptococci,Streptococcus pneumoniae, and Staphylococcus epidermidis showed low levels of binding. Bound MBL was able to promote C4 deposition in a concentration-dependent manner. We conclude that MBL may be of importance in first-line immune defense against several important pathogens.

scholarly journals L-Ficolin/Mannose-Binding Lectin-Associated Serine Protease Complexes Bind to Group B Streptococci Primarily through N-Acetylneuraminic Acid of Capsular Polysaccharide and Activate the Complement Pathway

2007 ◽  
Vol 76 (1) ◽  
pp. 179-188 ◽  
Author(s):  
Youko Aoyagi ◽  
Elisabeth E. Adderson ◽  
Craig E. Rubens ◽  
John F. Bohnsack ◽  
Jin G. Min ◽  
...  
Keyword(s):  
Serine Protease ◽  
Specific Antibody ◽  
Capsular Polysaccharide ◽  
Mannose Binding Lectin ◽  
Lectin Pathway ◽  
Group B Streptococci ◽  
Acetylneuraminic Acid ◽  
Mannose Binding ◽  
Group B ◽  
Binding Lectin

ABSTRACT Group B streptococci (GBS) are the most common cause of neonatal sepsis and meningitis. Most infants who are colonized with GBS at birth do not develop invasive disease, although many of these uninfected infants lack protective levels of capsular polysaccharide (CPS)-specific antibody. The lectin pathway of complement is a potential mechanism for initiating opsonization of GBS with CPS-specific antibody-deficient serum. In this study, we determined whether mannose-binding lectin (MBL)/MBL-associated serine protease (MASP) complexes and L-ficolin/MASP complexes bind to different strains of GBS to activate the lectin pathway, and we identified the molecules recognized by lectins on the GBS surface. We found that MBL did not bind to any GBS examined, whereas L-ficolin bound to GBS cells of many serotypes. L-ficolin binding to GBS cells correlated with the CPS content in serotypes Ib, III (restriction digestion pattern types III-2 and III-3), and V but not with the group B-specific polysaccharide (GBPS) content or with the lipoteichoic acid (LTA) content. L-ficolin bound to purified CPS and GBPS in a concentration-dependent manner but not to purified LTA. All strains to which L-ficolin/MASP complexes bound consumed C4. When N-acetylneuraminic acid (NeuNAc) was selectively removed from GBS cells by treatment with neuraminidase, the reduction in L-ficolin binding was correlated with the amount of NeuNAc removed. Additionally, L-ficolin was able to bind to wild-type strains but was able to bind only weakly to unencapsulated mutants and a mutant strain in which the CPS lacks NeuNAc. We concluded that L-ficolin/MASP complexes bind to GBS primarily through an interaction with NeuNAc of CPS.

scholarly journals Role of L-Ficolin/Mannose-Binding Lectin-Associated Serine Protease Complexes in the Opsonophagocytosis of Type III Group B Streptococci

2004 ◽  
Vol 174 (1) ◽  
pp. 418-425 ◽  
Author(s):  
Youko Aoyagi ◽  
Elisabeth E. Adderson ◽  
Jin G. Min ◽  
Misao Matsushita ◽  
Teizo Fujita ◽  
...  
Keyword(s):  
Serine Protease ◽  
Mannose Binding Lectin ◽  
Group B Streptococci ◽  
Type Iii ◽  
Mannose Binding ◽  
Group B ◽  
Binding Lectin

scholarly journals Mannose Binding Lectin Is Hydroxylated by Collagen Prolyl-4-hydroxylase and Inhibited by Some PHD Inhibitors

Kidney360 ◽  
2020 ◽  
Vol 1 (6) ◽  
pp. 447-457
Author(s):  
Vijesh J. Bhute ◽  
James Harte ◽  
Jack W. Houghton ◽  
Patrick H. Maxwell
Keyword(s):  
Immune Defense ◽  
Mannose Binding Lectin ◽  
Innate Immune ◽  
Significant Suppression ◽  
Post Translational Modifications ◽  
Innate Immune Defense ◽  
Mannose Binding ◽  
Prolyl Hydroxylation ◽  
Target Effect ◽  
Binding Lectin

BackgroundMannose-binding lectin (MBL) is an important component of innate immune defense. MBL undergoes oligomerization to generate high mol weight (HMW) forms which act as pattern recognition molecules to detect and opsonize various microorganisms. Several post-translational modifications including prolyl hydroxylation are known to affect the oligomerization of MBL. Yet, the enzyme(s) which hydroxylate proline in the collagen-like domain residues have not been identified and the significance of prolyl hydroxylation is incompletely understood.MethodsTo investigate post-translational modifications of MBL, we stably expressed Myc-DDK tagged MBL in HEK293S cells. We used pharmacologic and genetic inhibition of 2-oxoglutarate–dependent dioxygenases (2OGDD) to identify the enzyme required for prolyl hydroxylation of MBL. We performed mass spectrometry to determine the effects of various inhibitors on MBL modifications.ResultsSecretion of HMW MBL was impaired by inhibitors of the superfamily of 2OGDD, and was dependent on prolyl-4-hydroxylase subunit α1. Roxadustat and vadadustat, but not molidustat, led to significant suppression of hydroxylation and secretion of HMW forms of MBL.ConclusionsThese data suggest that prolyl hydroxylation in the collagen-like domain of MBL is mediated by collagen prolyl-4-hydroxylase. Reduced MBL activity is likely to be an off-target effect of some, but not all, prolyl hydroxylase domain (PHD) inhibitors. There may be advantages in selective PHD inhibitors that would not interfere with MBL production.

scholarly journals Mannose-binding lectin enhances Toll-like receptors 2 and 6 signaling from the phagosome

2008 ◽  
Vol 205 (1) ◽  
pp. 169-181 ◽  
Author(s):  
W.K. Eddie Ip ◽  
Kazue Takahashi ◽  
Kathryn J. Moore ◽  
Lynda M. Stuart ◽  
R. Alan B. Ezekowitz
Keyword(s):  
Defense Mechanisms ◽  
Immune Defense ◽  
Mannose Binding Lectin ◽  
Innate Immune ◽  
Toll Like Receptor ◽  
Cellular Environment ◽  
Mannose Binding ◽  
Toll Like Receptor 2 ◽  
Binding Lectin ◽  
Soluble Components

Innate immunity is the first-line defense against pathogens and relies on phagocytes, soluble components, and cell-surface and cytosolic pattern recognition receptors. Despite using hard-wired receptors and signaling pathways, the innate immune response demonstrates surprising specificity to different pathogens. We determined how combinatorial use of innate immune defense mechanisms defines the response. We describe a novel cooperation between a soluble component of the innate immune system, the mannose-binding lectin, and Toll-like receptor 2 that both specifies and amplifies the host response to Staphylococcus aureus. Furthermore, we demonstrate that this cooperation occurs within the phagosome, emphasizing the importance of engulfment in providing the appropriate cellular environment to facilitate the synergy between these defense pathways.

Low levels of mannose-binding lectin confers protection against tuberculosis in Turkish children

2008 ◽  
Vol 27 (12) ◽  
pp. 1165-1169 ◽  
Author(s):  
H. Cosar ◽  
F. Ozkinay ◽  
H. Onay ◽  
N. Bayram ◽  
A. R. Bakiler ◽  
...  
Keyword(s):  
Mannose Binding Lectin ◽  
Turkish Children ◽  
Mannose Binding ◽  
Low Levels ◽  
Binding Lectin

Mannose-binding lectin gene (MBL2) polymorphisms related to the mannose-binding lectin low levels are associated to dengue disease severity

2016 ◽  
Vol 77 (7) ◽  
pp. 571-575 ◽  
Author(s):  
Gabriela G. Figueiredo ◽  
Renata D. Cezar ◽  
Naishe M. Freire ◽  
Vanessa G. Teixeira ◽  
Paulo Baptista ◽  
...  
Keyword(s):  
Disease Severity ◽  
Mannose Binding Lectin ◽  
Dengue Disease ◽  
Lectin Gene ◽  
Mannose Binding ◽  
Low Levels ◽  
Binding Lectin

scholarly journals Mannose-Binding Lectin Gene Polymorphism and Its Association with Susceptibility to Recurrent Vulvovaginal Candidiasis

2018 ◽  
Vol 2018 ◽  
pp. 1-8 ◽  
Author(s):  
Noha M. Hammad ◽  
Nissreen E. El Badawy ◽  
Ashraf M. Nasr ◽  
Hamed A. Ghramh ◽  
Laila M. Al Kady
Keyword(s):  
Serum Level ◽  
Immune Defense ◽  
Vulvovaginal Candidiasis ◽  
Mannose Binding Lectin ◽  
Variant Allele ◽  
Recurrent Vulvovaginal Candidiasis ◽  
Mannose Binding ◽  
Exon 1 ◽  
Childbearing Women ◽  
Binding Lectin

Recurrent vulvovaginal candidiasis (RVVC) is a common illness influencing childbearing women worldwide. Most women suffering from RVVC develop infection without specified risk factors. Mannose-binding lectin (MBL) is an important component of innate immune defense against Candida infection. Innate immunity gene mutations and polymorphisms have been suggested to play a role in susceptibility to RVVC. This study aimed to investigate the association between MBL 2 gene exon 1 codon 54 polymorphism and susceptibility to RVVC in childbearing women. Whole blood and serum samples were obtained from 59 RVVC cases and 59 controls. MBL serum level was measured by enzyme-linked immune-sorbent assay (ELISA). MBL2 exon 1 codon 54 polymorphism was determined by polymerase chain reaction-restriction fragment length polymorphism (PCR-RFLP). It was shown that MBL serum level was nonsignificantly different between RVVC cases and controls. The risk of RVVC was 3 times higher in those carrying MBL2 exon 1 codon 54 variant allele (B). It could be concluded that the carrying of MBL2 exon 1 codon 54 variant allele (B) was shown to be a risk factor for RVVC in childbearing women.

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