Expression of the Carbohydrate Recognition Domain of Lung Surfactant Protein D and Demonstration of Its Binding to Lipopolysaccharides of Gram-Negative Bacteria

1994 ◽  
Vol 202 (3) ◽  
pp. 1674-1680 ◽  
Author(s):  
B.L. Lim ◽  
J.Y. Wang ◽  
U. Holmskov ◽  
H.J. Hoppe ◽  
K.B.M. Reid
Keyword(s):  
Lung Surfactant ◽  
Surfactant Protein ◽  
Surfactant Protein D ◽  
Carbohydrate Recognition Domain ◽  
Gram Negative Bacteria ◽  
Carbohydrate Recognition ◽  
Gram Negative ◽  
Lung Surfactant Protein

scholarly journals The α-helical neck region of human lung surfactant protein D is essential for the binding of the carbohydrate recognition domains to lipopolysaccharides and phospholipids

1996 ◽  
Vol 318 (2) ◽  
pp. 505-511 ◽  
Author(s):  
Uday KISHORE ◽  
Jiu-Yao WANG ◽  
Hans-Jürgen HOPPE ◽  
Kenneth B. M. REID
Keyword(s):  
Human Lung ◽  
Lung Surfactant ◽  
Neck Region ◽  
Surfactant Protein ◽  
Surfactant Protein D ◽  
Carbohydrate Binding ◽  
Carbohydrate Recognition ◽  
E Coli ◽  
Carbohydrate Recognition Domains ◽  
Lung Surfactant Protein

We have expressed the carbohydrate recognition domains (CRDs) of human lung surfactant protein D (SP-D) in Escherichia coli as a trimeric structure held together by the α-helical neck region of the molecule. The DNA sequence coding for the neck-region peptide and the CRD of SP-D was subcloned and expressed as a fusion protein containing the E. coli maltose binding protein (MBP). After removal of the MBP, the recombinant structure, containing three CRDs of SP-D, was found to be comparable to native SP-D in terms of carbohydrate binding specificity, the binding to lipopolysaccharides (LPSs) of Gram-negative bacteria, and interaction with phospholipids. The CRD of SP-D, without the neck region peptide, was also expressed and shown to behave as a monomer that showed a very weak affinity for maltose-agarose, LPSs and phospholipids. The α-helical neck region on its own showed affinity for phospholipids and thus might contribute to the binding of SP-D to these structures. However, the possibility that hydrophobic patches, which are exposed only in the isolated neck region and not in the intact SP-D, plays a role in neck region–phospholipid interaction, cannot be excluded. The results confirm the importance of the neck region as a trimerizing agent in bringing together three CRDs and suggest that multivalency is important in the strong binding of SP-D to carbohydrate targets.

scholarly journals Porcine Lung Surfactant Protein D: Complementary DNA Cloning, Chromosomal Localization, and Tissue Distribution

2000 ◽  
Vol 164 (3) ◽  
pp. 1442-1450 ◽  
Author(s):  
Martin van Eijk ◽  
Henk P. Haagsman ◽  
Thomas Skinner ◽  
Alan Archibold ◽  
Kenneth B. M. Reid ◽  
...  
Keyword(s):  
Tissue Distribution ◽  
Chromosomal Localization ◽  
Lung Surfactant ◽  
Surfactant Protein ◽  
Surfactant Protein D ◽  
Dna Cloning ◽  
Complementary Dna ◽  
Complementary Dna Cloning ◽  
Lung Surfactant Protein

Human surfactant protein D: SP-D contains a C-type lectin carbohydrate recognition domain

1991 ◽  
Vol 290 (1) ◽  
pp. 116-126 ◽  
Author(s):  
Kevin Rust ◽  
Leonard Grosso ◽  
Vivian Zhang ◽  
Donald Chang ◽  
Anders Persson ◽  
...  
Keyword(s):  
Surfactant Protein ◽  
Surfactant Protein D ◽  
Carbohydrate Recognition Domain ◽  
Carbohydrate Recognition

Dynamic Strength of the Interaction between Lung Surfactant Protein D (SP-D) and Saccharide Ligands†

Biochemistry ◽  
2007 ◽  
Vol 46 (43) ◽  
pp. 12231-12237 ◽  
Author(s):  
Esben Thormann ◽  
Jakob K. Dreyer ◽  
Adam C. Simonsen ◽  
Per L. Hansen ◽  
Søren Hansen ◽  
...  
Keyword(s):  
Lung Surfactant ◽  
Dynamic Strength ◽  
Surfactant Protein ◽  
Surfactant Protein D ◽  
Lung Surfactant Protein

scholarly journals Mechanism of Interaction Between Lung Surfactant Protein-D and Influenza A Virus Hemagglutinin

2012 ◽  
Vol 102 (3) ◽  
pp. 63a
Author(s):  
Boon Chong Goh ◽  
Xueqing Zou ◽  
Michael J. Rynkiewicz ◽  
Barbara A. Seaton ◽  
Klaus J. Schulten
Keyword(s):  
Influenza A Virus ◽  
Influenza A ◽  
Lung Surfactant ◽  
Surfactant Protein ◽  
Surfactant Protein D ◽  
Mechanism Of Interaction ◽  
Lung Surfactant Protein
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