Alanine Mutagenesis of Surfactant Protein A Reveals That Lipid Binding and pH-Dependent Liposome Aggregation Are Mediated by the Carbohydrate Recognition Domain†

Biochemistry ◽  
1997 ◽  
Vol 36 (45) ◽  
pp. 13963-13971 ◽  
Author(s):  
Francis X. McCormack ◽  
Jennifer Stewart ◽  
Dennis R. Voelker ◽  
Mamatha Damodarasamy
Keyword(s):  
Protein A ◽  
Surfactant Protein ◽  
Lipid Binding ◽  
Surfactant Protein A ◽  
Carbohydrate Recognition Domain ◽  
Carbohydrate Recognition ◽  
Ph Dependent

scholarly journals Interaction of SP-A (surfactant protein A) with bacterial rough lipopolysaccharide (Re-LPS), and effects of SP-A on the binding of Re-LPS to CD14 and LPS-binding protein

2005 ◽  
Vol 391 (1) ◽  
pp. 115-124 ◽  
Author(s):  
Ignacio García-Verdugo ◽  
Fernando Sánchez-Barbero ◽  
Katrin Soldau ◽  
Peter S. Tobias ◽  
Cristina Casals
Keyword(s):  
Binding Protein ◽  
Protein A ◽  
Fluorescence Analysis ◽  
Surfactant Protein ◽  
Lipid Binding ◽  
Coli Strain ◽  
Surfactant Protein A ◽  
Human Macrophage ◽  
Independent Manner ◽  
Lps Binding

SP-A (surfactant protein A) is a lipid-binding collectin primarily involved in innate lung immunity. SP-A interacts with the bacterial rough LPS (lipopolysaccharide) Re-LPS (Re595 mutant of LPS from Salmonella minnesota), but not with smooth LPS. In the present study, we first examined the characteristics of the interaction of human SP-A with Re-LPS. Fluorescence intensity and anisotropy measurements of FITC-labelled Re-LPS in the presence and absence of SP-A indicated that SP-A bound to Re-LPS in solution in a Ca2+-independent manner, with a dissociation constant of 2.8×10−8 M. In the presence of calcium, a high-mobility complex of SP-A and [3H]Rb-LPS (Rb mutant of LPS from Escherichia coli strain LCD 25) micelles was formed, as detected by sucrose density gradients. Re-LPS aggregation induced by SP-A was further characterized by light scattering. On the other hand, human SP-A inhibited TNF-α (tumour necrosis factor-α) secretion by human macrophage-like U937 cells stimulated with either Re-LPS or smooth LPS. We further examined the effects of human SP-A on the binding of Re-LPS to LBP (LPS-binding protein) and CD14. SP-A decreased the binding of Re-LPS to CD14, but not to LBP, as detected by cross-linking experiments with 125I-ASD-Re-LPS [125I-labelled sulphosuccinimidyl-2-(p-azidosalicylamido)-1,3-dithiopropionate derivative of Re-LPS] and fluorescence analysis with FITC-Re-LPS. When SP-A, LBP and CD14 were incubated together, SP-A reduced the ability of LBP to transfer 125I-ASD-Re-LPS to CD14. These SP-A effects were not due to the ability of SP-A to aggregate Re-LPS in the presence of calcium, since they were observed in both the absence and the presence of calcium. These studies suggest that SP-A could contribute to modulate Re-LPS responses by altering the competence of the LBP–CD14 receptor complex.

scholarly journals Elucidation of Lipid Binding Sites on Lung Surfactant Protein A Using X-ray Crystallography, Mutagenesis, and Molecular Dynamics Simulations

Biochemistry ◽  
2016 ◽  
Vol 55 (26) ◽  
pp. 3692-3701 ◽  
Author(s):  
Boon Chong Goh ◽  
Huixing Wu ◽  
Michael J. Rynkiewicz ◽  
Klaus Schulten ◽  
Barbara A. Seaton ◽  
...  
Keyword(s):  
Binding Sites ◽  
Lung Surfactant ◽  
Protein A ◽  
Surfactant Protein ◽  
Lipid Binding ◽  
Surfactant Protein A ◽  
X Ray ◽  
X Ray Crystallography ◽  
Lung Surfactant Protein ◽  
Dynamics Simulations

scholarly journals Crystal Structure of Trimeric Carbohydrate Recognition and Neck Domains of Surfactant Protein A

2003 ◽  
Vol 278 (44) ◽  
pp. 43254-43260 ◽  
Author(s):  
James F. Head ◽  
Tanya R. Mealy ◽  
Francis X. McCormack ◽  
Barbara A. Seaton
Keyword(s):  
Crystal Structure ◽  
Protein A ◽  
Surfactant Protein ◽  
Surfactant Protein A ◽  
Carbohydrate Recognition

scholarly journals Effect of Acidic pH on the Structure and Lipid Binding Properties of Porcine Surfactant Protein A

1998 ◽  
Vol 273 (24) ◽  
pp. 15183-15191 ◽  
Author(s):  
Miguel L. F. Ruano ◽  
Jesus Pérez-Gil ◽  
Cristina Casals
Keyword(s):  
Protein A ◽  
Surfactant Protein ◽  
Lipid Binding ◽  
Surfactant Protein A ◽  
Acidic Ph ◽  
Binding Properties
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