Mannose binding lectin plays a crucial role in innate immunity against yeast by enhanced complement activation and enhanced uptake of polymorphonuclear cells

Asbeck, Eveline C van; Hoepelman, Andy I. M.; Scharringa, Jelle; Herpers, Bjorn L.; Verhoef, J.

doi:10.1186/1471-2180-8-229

Cited by 90 publications

(81 citation statements)

References 46 publications

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“…By using this approach and using Mascot search, three main protein hits were identified with sequence ID of G3MZ19, F1N1Z8, and F1MCV8 ( Additionally, from the UniProt 12_11, it was mentioned that the sequence ID G3MZ19 is a member of the mannose-binding protein or mannose-binding lectin (MBL) family. Mannose-binding lectin is known to give an important contribution to innate immune defense (van Asbeck et al, 2008;Lambourne et al, 2009). Although less information is available regarding MBL and its role in the saliva of cattle, especially the Bali breed, the presence of MBL-like family in the saliva of Bali cattle possibly contributes to the innate immunity that works together with epithelial barriers around the oral cavity as the first line protection system against pathogens.…”

Section: Resultsmentioning

confidence: 99%

Proteomic Analysis of a 14.2 kDa Protein Isolated from Bali Cattle(Bos Sondaicus/Javanicus)Saliva Using Single Dimension Sodium Dodecyl Sulphate-Polyacrylamide Gel Electrophoresis and Matrix-Assisted Laser Desorption Ionization Time-of-Flight Tandem Mass Spectrometer

Depamede

2013

Italian Journal of Animal Science

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A 14.2 kDa protein isolated from Bali cattle (Bos sondaicus/javanicus) saliva has been reported to have a bactericidal activity. The aim of this study was to analyse the nature of a 14.2 kDa protein using single dimension (1-D) sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and matrix-assisted laser desorption ionization time-of-flight tandem mass spectrometer (MALDI TOF/TOF). The protein was isolated by means of polyethylene glycol (PEG)/sodium sulfate aqueous twophase system, and then determined by 12.5% SDS-PAGE. A band of 14.2 kDa was sliced and analysed by MALDI TOF/TOF mass spectrometer using a 5800 proteomics analyzer. Mascot search and National Center for Biotechnology Information (NCBI) Blast search revealed that the spot of 1-D SDS-PAGE consisted of three proteins: zymogen granule protein 16 homologue B, pancreatic adenocarcinoma upregulated factor-like, and prolactin-inducible protein homologue precursor. The three proteins have been observed in Bos taurus and other species such as mouse. The actual nature of the proteins and their function in Bali cattle (Bos sondaicus/javanicus), as well as the connection with the evolution of bovines need further analysis.

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Section: Resultsmentioning

confidence: 99%

Proteomic Analysis of a 14.2 kDa Protein Isolated from Bali Cattle(Bos Sondaicus/Javanicus)Saliva Using Single Dimension Sodium Dodecyl Sulphate-Polyacrylamide Gel Electrophoresis and Matrix-Assisted Laser Desorption Ionization Time-of-Flight Tandem Mass Spectrometer

Depamede

2013

Italian Journal of Animal Science

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“…Previously, binding of MBL has been observed to several bacteria and the fungi Candida albicans, C. neoformans, and A. fumigatus (40,41), promoting lectin pathway complement deposition on S. aureus, C. albicans, and C. neoformans (40,41). Similarly, L-ficolin/MASP complexes from patients were shown to recognize lipoteichoic acid from Grampositive bacteria such as S. aureus, Streptococcus pyogenes, and S. agalactiae to initiate lectin pathway-dependent C4 turnover (42,43).…”

Section: Discussionmentioning

confidence: 99%

Role of Ficolin-A and Lectin Complement Pathway in the Innate Defense against Pathogenic Aspergillus Species

et al. 2013

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Aspergillus species are saprophytic molds causing life-threatening invasive fungal infections in the immunocompromised host. Innate immune recognition, in particular, the mechanisms of opsonization and complement activation, has been reported to be an integral part of the defense against fungi. We have shown that the complement component ficolin-A significantly binds to Aspergillus conidia and hyphae in a concentration-dependent manner and was inhibited by N-acetylglucosamine and N-acetylgalactosamine. Calcium-independent binding to Aspergillus fumigatus and A. terreus was observed, but binding to A. flavus and A. niger was calcium dependent. Ficolin-A binding to conidia was increased under low-pH conditions, and opsonization led to enhanced binding of conidia to A549 airway epithelial cells. In investigations of the lectin pathway of complement activation, ficolin-A-opsonized conidia did not lead to lectin pathway-specific C4 deposition. In contrast, the collectin mannose binding lectin C (MBL-C) but not MBL-A led to efficient lectin pathway activation on A. fumigatus in the absence of ficolin-A. In addition, ficolin-A opsonization led to a modulation of the proinflammatory cytokine interleukin-8. We conclude that ficolin-A may play an important role in the innate defense against Aspergillus by opsonizing conidia, immobilizing this fungus through enhanced adherence to epithelial cells and modulation of inflammation. However, it appears that other immune pattern recognition molecules, i.e., those of the collectin MBL-C, are involved in the Aspergillus-lectin complement pathway activation rather than ficolin-A.

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“…MBL has been shown to bind strongly to C. albicans through mannan, thus, resulting in complement activation and subsequent opsonophagocytosis by PMNs (31,44). To further extend and elucidate the physiological relevance of MBL collaboration with PTX3 and SAP, we performed phagocytosis experiments of C. albicans by PMNs using either MBL-defect serum that was depleted for SAP or C1q-defect serum that was depleted for MBL and SAP.…”

Section: Discussionmentioning

confidence: 99%

Heterocomplexes of Mannose-binding Lectin and the Pentraxins PTX3 or Serum Amyloid P Component Trigger Cross-activation of the Complement System

Jie

Doni

Skjoedt

et al. 2011

Journal of Biological Chemistry

111

123

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The long pentraxin 3 (PTX3), serum amyloid P component (SAP), and C-reactive protein belong to the pentraxin family of pattern recognition molecules involved in tissue homeostasis and innate immunity. They interact with C1q from the classical complement pathway. Whether this also occurs via the analogous mannose-binding lectin (MBL) from the lectin complement pathway is unknown. Thus, we investigated the possible interaction between MBL and the pentraxins. We report that MBL bound PTX3 and SAP partly via its collagen-like domain but not C-reactive protein. MBL-PTX3 complex formation resulted in recruitment of C1q, but this was not seen for the MBL-SAP complex. However, both MBL-PTX3 and MBL-SAP complexes enhanced C4 and C3 deposition and opsonophagocytosis of Candida albicans by polymorphonuclear leukocytes. Interaction between MBL and PTX3 led to communication between the lectin and classical complement pathways via recruitment of C1q, whereas SAP-enhanced complement activation occurs via a hitherto unknown mechanism. Taken together, MBL-pentraxin heterocomplexes trigger cross-activation of the complement system.

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Mannose binding lectin plays a crucial role in innate immunity against yeast by enhanced complement activation and enhanced uptake of polymorphonuclear cells

Cited by 90 publications

References 46 publications

Proteomic Analysis of a 14.2 kDa Protein Isolated from Bali Cattle(Bos Sondaicus/Javanicus)Saliva Using Single Dimension Sodium Dodecyl Sulphate-Polyacrylamide Gel Electrophoresis and Matrix-Assisted Laser Desorption Ionization Time-of-Flight Tandem Mass Spectrometer

Proteomic Analysis of a 14.2 kDa Protein Isolated from Bali Cattle(Bos Sondaicus/Javanicus)Saliva Using Single Dimension Sodium Dodecyl Sulphate-Polyacrylamide Gel Electrophoresis and Matrix-Assisted Laser Desorption Ionization Time-of-Flight Tandem Mass Spectrometer

Role of Ficolin-A and Lectin Complement Pathway in the Innate Defense against Pathogenic Aspergillus Species

Heterocomplexes of Mannose-binding Lectin and the Pentraxins PTX3 or Serum Amyloid P Component Trigger Cross-activation of the Complement System

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