Characterization and Quantification of Mouse Mannan‐Binding Lectins (MBL‐A and MBL‐C) and Study of Acute Phase Responses

Liu, H.; Jensen, Lisbeth; Hansen, Søren Gustenhoff; Petersen, Steen V.; Takahashi, Kazue; Ezekowitz, Alan; Hansen, Frederik Teilfeldt; Jensenius, Jens C.; Thiel, Steffen

doi:10.1046/j.1365-3083.2001.00908.x

Cited by 86 publications

(82 citation statements)

References 25 publications

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“…MBL is known to bind to unmodified Sepharose TM [40,41], consisting of agarose. This binding was inhibited by 0.2 M mannose in the same Ca 2+ -containing buffer (not shown), indicating that the binding occurs through the carbohydrate recognition domain of MBL as previously reported [42]. It was unexpected and interesting that around a half of peak 1 in type 3 (heterozygote) was eluted from the column.…”

Section: Discussionsupporting

confidence: 79%

Relationship between gene polymorphisms of mannose‐binding lectin (MBL) and two molecular forms of MBL

et al. 2003

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Mannose-binding lectin (MBL) activates complement through MBL-associated serine proteases (MASP). A deficiency in MBL due to mutations at exon 1 of the human MBL gene is reported to cause vulnerability to infection. We examined sera of known MBL genotype by gel filtration and assessed their elution patterns using an ELISA for MBL and identified two MBL forms, a high-molecular-mass form and a lower-molecular-mass form. By the identification of either or both forms in individual sera, three types of patterns emerged: type 1 consisted of a high-molecular form; type 2, of a low-molecular form; and type 3, of both forms. Types 1, 2 and 3 corresponded, respectively, to a wild type (A/A), a homozygous mutation at codon 54 (B/B) and their heterozygote (A/B). One exception was a heterozygous LXPA/LYPB phenotype that exhibited the type-2 pattern. Binding to mannan and MASP-1/3 occurred exclusively with the high-molecular form. An apparent MBL deficiency does not in fact represent a deficiency in MBL molecules but rather the presence of circulating oligomeric mutant MBL with impaired function.

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Section: Discussionsupporting

confidence: 79%

Relationship between gene polymorphisms of mannose‐binding lectin (MBL) and two molecular forms of MBL

et al. 2003

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“…To test this possibility, we used a time-resolved immunofluorometric assay-based binding assay (62). Monoclonal murine IgMs were immobilized in polystyrene plates followed by the addition of purified murine MBL-C or MBL-A protein.…”

Section: Resultsmentioning

confidence: 99%

“…Monoclonal murine IgMs were immobilized in polystyrene plates followed by the addition of purified murine MBL-C or MBL-A protein. The bound MBL on immobilized IgM were detected by specific Ab against MBL (62). To verify whether the binding depended on Ca 2ϩ , 1 mM CaCl 2 , or 5 mM EDTA, was added to the buffer.…”

Section: Resultsmentioning

confidence: 99%

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Activation of the Lectin Pathway by Natural IgM in a Model of Ischemia/Reperfusion Injury

Zhang

Takahashi

Alicot

et al. 2006

The Journal of Immunology

128

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Reperfusion of ischemic tissues elicits an acute inflammatory response involving serum complement, which is activated by circulating natural IgM specific to self-Ags exposed by ischemia. Recent reports demonstrating a role for the lectin pathway raise a question regarding the initial events in complement activation. To dissect the individual roles of natural IgM and lectin in activation of complement, mice bearing genetic deficiency in early complement, IgM, or mannan-binding lectin were characterized in a mesenteric model of ischemia reperfusion injury. The results reveal that IgM binds initially to ischemic Ag providing a binding site for mannan-binding lectin which subsequently leads to activation of complement and injury.

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“…MBL-A and MBL-C in the WT mouse serum and the supernatant were quantified to determine total MBL-A and MBL-C and unbound MBL-A and MBL-C using assays previously described (32). rhMBL in the supernatant was determined to quantify unbound rhMBL as previously described (33).…”

Section: Assay For Bacterial Growth In Whole Blood and Plasmamentioning

confidence: 99%

Deficiency of Mannose-Binding Lectin Greatly Increases Susceptibility to Postburn Infection withPseudomonas aeruginosa

Møller-Kristensen

Ip²,

Shi³

et al. 2006

The Journal of Immunology

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Burn injury disrupts the mechanical and biological barrier that the skin presents against infection by symbionts like the Pseudomonas aeruginosa, a Gram-negative bacteria. A combination of local factors, antimicrobial peptides, and resident effector cells form the initial response to mechanical injury of the skin. This activity is followed by an inflammatory response that includes influx of phagocytes and serum factors, such as complement and mannose-binding lectin (MBL), which is a broad-spectrum pattern recognition molecule that plays a key role in innate immunity. A growing consensus from studies in humans and mice suggests that lack of MBL together with other comorbid factors predisposes the host to infection. In this study we examined whether MBL deficiency increases the risk of P. aeruginosa infection in a burned host. We found that both wild-type and MBL null mice were resistant to a 5% total body surface area burn alone or s.c. infection with P. aeruginosa alone. However, when mice were burned then inoculated s.c. with P. aeruginosa at the burn site, all MBL null mice died by 42 h from septicemia, whereas only one-third of wild-type mice succumbed (p = 0.0005). This result indicates that MBL plays a key role in containing and preventing a systemic spread of P. aeruginosa infection following burn injury and suggests that MBL deficiency in humans maybe a premorbid variable in the predisposition to infection in burn victims.

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Characterization and Quantification of Mouse Mannan‐Binding Lectins (MBL‐A and MBL‐C) and Study of Acute Phase Responses

Cited by 86 publications

References 25 publications

Relationship between gene polymorphisms of mannose‐binding lectin (MBL) and two molecular forms of MBL

Relationship between gene polymorphisms of mannose‐binding lectin (MBL) and two molecular forms of MBL

Activation of the Lectin Pathway by Natural IgM in a Model of Ischemia/Reperfusion Injury

Deficiency of Mannose-Binding Lectin Greatly Increases Susceptibility to Postburn Infection withPseudomonas aeruginosa

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