High-resolution Structural Insights into Ligand binding and Immune Cell Recognition by Human Lung Surfactant Protein D

Shrive, A.K.; Tharia, Hazel A.; Strong, Peter; Kishore, Uday; Burns, I.; Rizkallah, P.J.; Reid, Kenneth B.M.; Greenhough, Trevor J.

doi:10.1016/s0022-2836(03)00761-7

Cited by 109 publications

(146 citation statements)

References 37 publications

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“…Calcium-dependent alterations in the CD spectrum of SP-D have also been described, providing further evidence for calcium-dependent conformational changes (50). Because the calcium binding sites differ in affinity (43), their differential occupancy could also influence susceptibility to degradation.…”

Section: Discussionmentioning

confidence: 85%

“…6). A coordinated Ca 2ϩ ion is integral to the primary carbohydrate binding site of collectins and most other C-type lectins (41), and three additional Ca 2ϩ binding sites have been identified within the CRDs based on the crystal structure of rfhSP-D (42,43). The Ca 2ϩ ions that are not directly involved in coordinating sugars are likely to influence protein structure and, thus, could potentially alter accessibility to Der p 1 and Der f 1, accounting for the decreased cleavage of SP-D and rfhSP-D in the presence of calcium.…”

Section: Discussionmentioning

confidence: 99%

“…Enhanced in the Absence of Calcium-Calcium ions are integral to the structure of the CRDs of both SP-A and SP-D (41)(42)(43)(44). Therefore, to determine whether the absence of calcium and any consequent changes in structure of the collectins could influence the allergen-induced degradation of collectins, NhSP-A, NhSP-D, and rfhSP-D were incubated with Der p 1 and Der f 1 in the absence of calcium, and cleavage products were resolved by SDS-PAGE (Fig.…”

Section: Degradation Of Sp-d But Not Sp-a Ismentioning

confidence: 99%

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Major House Dust Mite Allergens Dermatophagoides pteronyssinus 1 and Dermatophagoides farinae 1 Degrade and Inactivate Lung Surfactant Proteins A and D

Deb

Shakib

Reid

et al. 2007

Journal of Biological Chemistry

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Section: Discussionmentioning

confidence: 85%

Section: Discussionmentioning

confidence: 99%

Section: Degradation Of Sp-d But Not Sp-a Ismentioning

confidence: 99%

See 1 more Smart Citation

Major House Dust Mite Allergens Dermatophagoides pteronyssinus 1 and Dermatophagoides farinae 1 Degrade and Inactivate Lung Surfactant Proteins A and D

Deb

Shakib

Reid

et al. 2007

Journal of Biological Chemistry

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“…The common spatial arrangement of the ligand-binding sites on each of the proteins suggests that such an arrangement is universally required to recognize pathogen-associated molecular patterns (49) and that a triangle of this size is a basic trivalent recognition unit for general pathogens. Although GlcNAc is a common ligand for ficolins and collectins, collectins recognize the vicinal, equatorial 3-and 4-OH groups of sugars through a Ca 2ϩ (11,50), whereas L-ficolin and M-ficolin mainly recognize the acetamido group of GlcNAc, as predicted from the case of TL5A (34). Since the corresponding residues of the ligandbinding site in H-ficolin differ from those in L-ficolin, Mficolin, and TL5A, its manner of ligand binding may differ.…”

Section: Discussionmentioning

confidence: 99%

Trivalent Recognition Unit of Innate Immunity System

Tanio

Kondo

Sugio

et al. 2007

Journal of Biological Chemistry

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Ficolins are a kind of pathogen-recognition molecule in the innate immune systems. To investigate the discrimination mechanism between self and non-self by ficolins, we determined the crystal structure of the human M-ficolin fibrinogen-like domain (FD1), which is the ligand-binding domain, at 1.9 Å resolution. Although the FD1 monomer shares a common fold with the fibrinogen ␥ fragment and tachylectin-5A, the Asp-282-Cys-283 peptide bond, which is the predicted ligand-binding site on the C-terminal P domain, is a normal trans bond, unlike the cases of the other two proteins. The trimeric formation of FD1 results in the separation of the three P domains, and the spatial arrangement of the three predicted ligand-binding sites on the trimer is very similar to that of the trimeric collectin, indicating that such an arrangement is generally required for pathogen-recognition. The ligand binding study of FD1 in solution indicated that the recombinant protein binds to N-acetyl-D-glucosamine and the peptide Gly-Pro-Arg-Pro and suggested that the ligand-binding region exhibits a conformational equilibrium involving cis-trans isomerization of the Asp-282-Cys-283 peptide bond. The crystal structure and the ligand binding study of FD1 provide an insight of the self-and non-self discrimination mechanism by ficolins.Surveillance systems of innate immunity are present in all multicellular organisms and play a crucial role in the first line of defense against pathogens. Ficolins, as well as collectins, are one of the most important groups of pattern recognition molecules in the innate immunity systems (1-7) and have been identified in both vertebrates and invertebrates (6). Ficolins are comprised of a collagen-like domain at the N terminus and a fibrinogen-like domain (FBG), 3 which is the sugar-binding site, at the C terminus (8, 9). Collectins, such as mannose-binding lectin (MBL), lung surfactant protein A, and surfactant protein D, also consist of an N-terminal collagen-like domain and a C-terminal carbohydrate-recognition domain (CRD) that binds to certain carbohydrates such as mannose and GlcNAc Ca 2ϩ dependently. The CRD on MBL, surfactant protein A, and surfactant protein D forms a trimeric structure through a triple ␣-helical coiled-coil at a short neck region between the collagen-like domain and the CRD (10 -12). Ficolins also form trimers (8,13,14), although the mechanism of trimerization is unclear. Both ficolins and collectins form trimer-based multimers that are N-terminally linked by disulfide bonds (15). Ficolins and MBL also interact with MBL-associated serine proteases, and their complexes activate the lectin complement pathway (6, 16 -23).Ficolins were originally discovered in porcine uterus membrane extracts as transforming growth factor-␤-binding proteins (24,25). In human, L-ficolin and H-ficolin in serum and M-ficolin in cells have been characterized (9, 14, 26 -29). Lficolin (synonymous with ficolin-2 or Ficolin/P35) binds to GlcNAc (29, 30) and GalNAc (8). The binding ability is inhibited by acetylated c...

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“…A recent crystallographic study upon the lung surfactant protein D (SP-D), a protein capable of interacting directly with carbohydrate residues on pulmonary pathogens and allergens, of stimulating immune cells and of intervening directly in the lungs' immune response, has revealed that a previously unreported calcium ion is essential for biological activity, ensuring the right structural requirements for the established effector mechanism. 120 The lectin from Vatairea macrocarpa seeds (VML) was used to induce neutrophil migration in rats in order to explore the pathways by which lectins cause an inflammatory response. 121 The results obtained suggested that the lectin-induced effects do not involve the usual mediators, such as PAF mediator, rather it acts through an indirect mechanism.…”

Section: Diagnostic and Therapeutic Applicationsmentioning

confidence: 99%

Lectins: Tools for the Molecular Understanding of the Glycocode

2005

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Recent progress in glycobiology has revealed that cell surface oligosaccharides play an essential role in recognition events. More precisely, these saccharides may be complexed by lectins, carbohydrate-binding proteins other than enzymes and antibodies, able to recognise sugars in a highly specific manner. The ubiquity of lectin-carbohydrate interactions opens enormous potential for their exploitation in BA (1993) and DPhil (1996) T h i s j o u r n a l i s © T h e R o y a l S o c i e t y o f C h e m i s t r y

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High-resolution Structural Insights into Ligand binding and Immune Cell Recognition by Human Lung Surfactant Protein D

Cited by 109 publications

References 37 publications

Major House Dust Mite Allergens Dermatophagoides pteronyssinus 1 and Dermatophagoides farinae 1 Degrade and Inactivate Lung Surfactant Proteins A and D

Major House Dust Mite Allergens Dermatophagoides pteronyssinus 1 and Dermatophagoides farinae 1 Degrade and Inactivate Lung Surfactant Proteins A and D

Trivalent Recognition Unit of Innate Immunity System

Lectins: Tools for the Molecular Understanding of the Glycocode

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