Site-specific N-glycan characterization of human complement factor H

Fenaille, François; Mignon, Maxime Le; Groseil, Catherine; Ramon, C.; Riandé, Sandrine; Siret, L.; Bihoreau, Nicolas

doi:10.1093/glycob/cwm060

Cited by 60 publications

(70 citation statements)

References 40 publications

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“…There has been a recent interest in studying glycosylation of complement components, and in some instances glycosylation is important for the function of these proteins (11,19,44,46,56). Most complement components are synthesized predominantly in the liver and contain complex biantennary glycans, as displayed in Fig.…”

Section: Discussionmentioning

confidence: 99%

Three Surface Exoglycosidases fromStreptococcus pneumoniae, NanA, BgaA, and StrH, Promote Resistance to Opsonophagocytic Killing by Human Neutrophils

Dalia¹,

Standish²,

2010

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Streptococcus pneumoniae (the pneumococcus) is a major human pathogen and a leading cause of inflammatory infections such as pneumonia and otitis media. An important mechanism for host defense against S. pneumoniae is opsonophagocytic killing by neutrophils. To persist in the human host, the pneumococcus has developed strategies to evade opsonization and subsequent neutrophil-mediated killing. Utilizing a genomic approach, we identified NanA, the major pneumococcal neuraminidase, as a factor important for resistance to opsonophagocytic killing in ex vivo killing assays using human neutrophils. The effect of NanA was shown using both type 4 (TIGR4) and type 6A clinical isolates. NanA promotes this resistance by acting in conjunction with two other surface-associated exoglycosidases, BgaA, a ␤-galactosidase, and StrH, an N-acetylglucosaminidase. Experiments using human serum showed that these exoglycosidases reduced deposition of complement component C3 on the pneumococcal surface, providing a mechanism for this resistance. Additionally, we have shown that antibodies in human serum do not contribute to this phenotype. These results demonstrate that deglycosylation of a human serum glycoconjugate(s) by the combined effects of NanA, BgaA, and StrH, is important for resistance to complement deposition and subsequent phagocytic killing of S. pneumoniae.

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Section: Discussionmentioning

confidence: 99%

Three Surface Exoglycosidases fromStreptococcus pneumoniae, NanA, BgaA, and StrH, Promote Resistance to Opsonophagocytic Killing by Human Neutrophils

Dalia¹,

Standish²,

2010

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“…The FH amino acid composition was taken from its sequence (Swiss-Prot accession code P08603). The glycosylation of FH was taken to be eight biantennary oligosaccharides located at SCR-9, SCR-12, SCR-13, SCR-14, SCR-15 (two sites), SCR-17, and SCR-18; note that SCR-4 is not glycosylated (36). This composition resulted in a calculated FH molecular mass of 154.4 kDa, an unhydrated volume of 193.1 nm 3 , a hydrated volume of 256.2 nm 3 (based on a hydration of 0.3 g of H 2 O/g of glycoprotein and an electrostricted volume of 0.0245 nm 3 /bound water molecule), a partial specific volume (v ) of 0.715 ml/g, and an absorption coefficient at 280 nm (1%, 1-cm path length) of 16.2 (13,37).…”

Section: Methodsmentioning

confidence: 99%

Complement Factor H Binds at Two Independent Sites to C-reactive Protein in Acute Phase Concentrations*

Okemefuna¹,

Nan²,

Miller³

et al. 2010

Journal of Biological Chemistry

113

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Factor H (FH) regulates the activation of C3b in the alternative complement pathway, both in serum and at host cell surfaces. It is composed of 20 short complement regulator (SCR) domains. The Y402H polymorphism in FH is a risk factor for age-related macular degeneration. C-reactive protein (CRP) is an acute phase protein that binds Ca 2؉ . We established the FH-CRP interaction using improved analytical ultracentrifugation (AUC), surface plasmon resonance (SPR), and synchrotron x-ray scattering methods. Physiological FH and CRP concentrations were used in 137 mM NaCl and 2 mM Ca 2؉ , in which the occurrence of denatured CRP was avoided. In solution, AUC revealed FH-CRP binding. The FH-CRP interaction inhibited the formation of higher FH oligomers, indicating that CRP blocked FH dimerization sites at both SCR-6/8 and SCR-16/20. SPR confirmed the FH-CRP interaction and its NaCl concentration dependence upon using either immobilized FH or CRP. The SCR-1/5 fragment of FH did not bind to CRP. In order of increasing affinity, SCR-16/20, SCR-6/8 (His-402), and SCR-6/8 (Tyr-402) fragments bound to CRP. X-ray scattering showed that FH became more compact when binding to CRP, which is consistent with CRP binding at two different FH sites. We concluded that FH and CRP bind at elevated acute phase concentrations of CRP in physiological buffer. The SCR-16/20 site is novel and indicates the importance of the FH-CRP interaction for both age-related macular degeneration and atypical hemolytic uremic syndrome.

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“…Glycan mass by difference. (Fenaille, et al, 2007b) Egg-secreted protein Structural determination of high-mannose and paucimannosidic glycans (Sandra, et al, 2007) HIV Envelope proteins -…”

Section: Pngase F R-tof (Dhb) Glycans Esi-ms/ms (Negative Ion)mentioning

confidence: 99%

Analysis of carbohydrates and glycoconjugates by matrix‐assisted laser desorption/ionization mass spectrometry: An update for 2007–2008

Harvey

2011

Mass Spectrometry Reviews

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This review is the fifth update of the original review, published in 1999, on the application of MALDI mass spectrometry to the analysis of carbohydrates and glycoconjugates and brings coverage of the literature to the end of 2008. The first section of the review covers fundamental studies, fragmentation of carbohydrate ions, use of derivatives and new software developments for analysis of carbohydrate spectra. Among newer areas of method development are glycan arrays, MALDI imaging and the use of ion mobility spectrometry. The second section of the review discusses applications of MALDI MS to the analysis of different types of carbohydrate. Specific compound classes that are covered include carbohydrate polymers from plants, N- and O-linked glycans from glycoproteins, biopharmaceuticals, glycated proteins, glycolipids, glycosides and various other natural products. There is a short section on the use of MALDI mass spectrometry for the study of enzymes involved in glycan processing and a section on the use of MALDI MS to monitor products of the chemical synthesis of carbohydrates with emphasis on carbohydrate-protein complexes and glycodendrimers. Corresponding analyses by electrospray ionization now appear to outnumber those performed by MALDI and the amount of literature makes a comprehensive review on this technique impractical. However, most of the work relating to sample preparation and glycan synthesis is equally relevant to electrospray and, consequently, those proposing analyses by electrospray should also find material in this review of interest.

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Site-specific N-glycan characterization of human complement factor H

Cited by 60 publications

References 40 publications

Three Surface Exoglycosidases fromStreptococcus pneumoniae, NanA, BgaA, and StrH, Promote Resistance to Opsonophagocytic Killing by Human Neutrophils

Three Surface Exoglycosidases fromStreptococcus pneumoniae, NanA, BgaA, and StrH, Promote Resistance to Opsonophagocytic Killing by Human Neutrophils

Complement Factor H Binds at Two Independent Sites to C-reactive Protein in Acute Phase Concentrations*

Analysis of carbohydrates and glycoconjugates by matrix‐assisted laser desorption/ionization mass spectrometry: An update for 2007–2008

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