scholarly journals Distinctive anti-influenza properties of recombinant collectin 43

2002 ◽  
Vol 366 (1) ◽  
pp. 87-96 ◽  
Author(s):  
Kevan L. HARTSHORN ◽  
Uffe HOLMSKOV ◽  
Soren HANSEN ◽  
Pengnian ZHANG ◽  
Joseph MESCHI ◽  
...  
Keyword(s):  
Mammalian Cells ◽  
Influenza A ◽  
Antimicrobial Properties ◽  
Surfactant Protein ◽  
Surfactant Protein D ◽  
Bacterial Aggregation ◽  
Structural And Functional Properties ◽  
Antiviral Activities ◽  
Innate Defence

Collectins play important roles in innate defence against viral, fungal and bacterial pathogens. CL-43, a bovine serum collectin, which appears to have evolutionarily evolved from surfactant protein D (SP-D), shows unique structural and functional properties. In the present study, we describe the initial characterization of a recombinant CL-43 expressed in mammalian cells. Like natural CL-43, the recombinant is secreted as trimeric forms that show a preference for mannose and N-acetyl mannosamine. The natural and recombinant proteins have significantly higher haemagglutination-inhibiting activity against influenza A virus (IAV) than recombinant trimeric forms of SP-D. In contrast with the more highly multimerized forms of SP-D, namely conglutinin or mannose-binding lectin, CL-43 did not induce viral or bacterial aggregation and did not enhance IAV-induced neutrophil H2O2 generation. Like SP-D, CL-43 also strongly enhanced neutrophil uptake of IAV. However, the mechanism of this enhanced internalization is different from that of SP-D in that it did not require viral aggregation. These studies establish that the trimeric structure of CL-43 is specified by its primary sequence and indicate that this naturally occurring trimeric collectin has unique antiviral activities. These findings could facilitate the development of recombinant collectins with novel antimicrobial properties.

scholarly journals Salivary agglutinin and lung scavenger receptor cysteine-rich glycoprotein 340 have broad anti-influenza activities and interactions with surfactant protein D that vary according to donor source and sialylation

2005 ◽  
Vol 393 (2) ◽  
pp. 545-553 ◽  
Author(s):  
Kevan L. Hartshorn ◽  
Antoon Ligtenberg ◽  
Mitchell R. White ◽  
Martin van Eijk ◽  
Max Hartshorn ◽  
...  
Keyword(s):  
Antiviral Activity ◽  
Influenza A ◽  
Scavenger Receptor ◽  
Surfactant Protein ◽  
Sialic Acids ◽  
Surfactant Protein D ◽  
Influenza A Viruses ◽  
Viral Neutralization ◽  
Antiviral Activities ◽  
Innate Defence

We previously found that scavenger receptor cysteine-rich gp-340 (glycoprotein-340), isolated from lung or saliva, directly inhibits human IAVs (influenza A viruses). We now show that salivary gp-340 has broad antiviral activity against human, equine and porcine IAV strains. Although lung and salivary gp-340 are identical in protein sequence, salivary gp-340 from one donor had significantly greater antiviral activity against avian-like IAV strains which preferentially bind sialic acids in α(2,3) linkage. A greater density of α(2,3)-linked sialic acids was present on the salivary gp-340 from this donor as compared with salivary gp-340 from another donor or several preparations of lung gp-340. Hence, the specificity of sialic acid linkages on gp-340 is an important determinant of anti-IAV activity. Gp-340 binds to SP-D (surfactant protein D), and we previously showed that lung gp-340 has co-operative interactions with SP-D in viral neutralization and aggregation assays. We now report that salivary gp-340 can, in some cases, strongly antagonize certain antiviral activities of SP-D. This effect was associated with greater binding of salivary gp-340 to the carbohydrate recognition domain of SP-D as compared with the binding of lung gp-340. These findings may relate to inter-individual variations in innate defence against highly pathogenic IAV and to effects of aspiration of oral contents on SP-D-mediated lung functions.

scholarly journals Pulmonary Surfactant Protein D in First-Line Innate Defence against Influenza A Virus Infections

2013 ◽  
Vol 5 (3) ◽  
pp. 197-208 ◽  
Author(s):  
Marine L.B. Hillaire ◽  
Henk P. Haagsman ◽  
Albert D.M.E. Osterhaus ◽  
Guus F. Rimmelzwaan ◽  
Martin van Eijk
Keyword(s):  
Influenza A Virus ◽  
Pulmonary Surfactant ◽  
Influenza A ◽  
Surfactant Protein ◽  
Surfactant Protein D ◽  
Virus Infections ◽  
First Line ◽  
Innate Defence ◽  
Pulmonary Surfactant Protein

scholarly journals Expression of Surfactant protein D (SP-D) distinguishes severe pandemic influenza A(H1N1) from COVID-19

2021 ◽  
Author(s):  
José Alberto Choreño-Parra ◽  
Luis Armando Jiménez-Álvarez ◽  
Gustavo Ramírez-Martínez ◽  
Alfredo Cruz-Lagunas ◽  
Mahima Thapa ◽  
...  
Keyword(s):  
Pandemic Influenza ◽  
Influenza A ◽  
Alveolar Epithelium ◽  
Surfactant Protein ◽  
High Serum ◽  
Surfactant Protein D ◽  
Diagnostic Challenge ◽  
Moderate Disease ◽  
Influenza A H1n1 ◽  
Novel Biomarkers

Abstract The differentiation of influenza and COVID-19 could constitute a diagnostic challenge during the ongoing winter due to their clinical similitude. Thus, novel biomarkers that enable distinguishing both diseases are required. Here, we evaluated whether the surfactant protein D (SP-D), a collectin produced at the alveolar epithelium with known immune properties, was useful to differentiate pandemic influenza A(H1N1) from COVID-19 in critically ill patients. Our results revealed high serum SP-D levels in severe pandemic influenza but not COVID-19 patients. This finding was validated in a separate cohort of mechanically ventilated COVID-19 patients who also showed low plasma SP-D levels. However, plasma SP-D levels did not distinguish seasonal influenza from COVID-19 in mild-to-moderate disease. Finally, we found that high serum SP-D levels were associated with mortality and renal failure among severe pandemic influenza cases. Thus, our studies have identified SP-D as a unique biomarker expressed during severe pandemic influenza but not COVID-19.

scholarly journals Lectin-mediated binding and sialoglycans of porcine surfactant protein D synergistically neutralize influenza A virus

2018 ◽  
Vol 293 (27) ◽  
pp. 10646-10662 ◽  
Author(s):  
Martin van Eijk ◽  
Michael J. Rynkiewicz ◽  
Kshitij Khatri ◽  
Nancy Leymarie ◽  
Joseph Zaia ◽  
...  
Keyword(s):  
Influenza A Virus ◽  
Influenza A ◽  
Surfactant Protein ◽  
Surfactant Protein D

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

scholarly journals Identification and Characterization of a Novel Interaction between Pulmonary Surfactant Protein D and Decorin

2003 ◽  
Vol 278 (28) ◽  
pp. 25678-25687 ◽  
Author(s):  
Jeya Nadesalingam ◽  
Andrés López Bernal ◽  
Alister W. Dodds ◽  
Antony C. Willis ◽  
David J. Mahoney ◽  
...  
Keyword(s):  
Pulmonary Surfactant ◽  
Surfactant Protein ◽  
Surfactant Protein D ◽  
Identification And Characterization ◽  
Pulmonary Surfactant Protein

scholarly journals The human cathelicidin LL-37 inhibits influenza A viruses through a mechanism distinct from that of surfactant protein D or defensins

2013 ◽  
Vol 94 (1) ◽  
pp. 40-49 ◽  
Author(s):  
Shweta Tripathi ◽  
Tesfaldet Tecle ◽  
Anamika Verma ◽  
Erika Crouch ◽  
Mitchell White ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Epithelial Cells ◽  
Antiviral Activity ◽  
Influenza A ◽  
Density Lipoprotein ◽  
Surfactant Protein ◽  
Host Defence ◽  
Surfactant Protein D ◽  
Influenza A Viruses ◽  
Cationic Antimicrobial Peptide

LL-37, the only human cathelicidin, is a cationic antimicrobial peptide with antibacterial and antifungal activity. LL-37 is released from neutrophil granules and produced by epithelial cells. It has been implicated in host defence against influenza A virus (IAV) in recent studies. We now demonstrate dose-related neutralizing activity of LL-37 against several seasonal and mouse-adapted IAV strains. The ability of LL-37 to inhibit these IAV strains resulted mainly from direct effects on the virus, since pre-incubation of virus with LL-37 was needed for optimal inhibition. LL-37 bound high-density lipoprotein (HDL), and pre-incubation of LL-37 with human serum or HDL reduced its antiviral activity. LL-37 did not inhibit viral association with epithelial cells as assessed by quantitative RT-PCR or confocal microscopy. This finding contrasted with results obtained with surfactant protein D (SP-D). Unlike collectins or human neutrophil defensins (HNPs), LL-37 did not induce viral aggregation under electron microscopy. In the electron microscopy studies, LL-37 appeared to cause disruption of viral membranes. LL-37 had additive antiviral activity when combined with other innate inhibitors like SP-D, surfactant protein A and HNPs. Unlike HNPs, LL-37 did not bind SP-D significantly. These findings indicate that LL-37 contributes to host defence against IAV through a mechanism distinct from that of SP-D and HNPs.

scholarly journals Mutagenesis of Surfactant Protein D Informed by Evolution and X-ray Crystallography Enhances Defenses against Influenza A Virusin Vivo

2011 ◽  
Vol 286 (47) ◽  
pp. 40681-40692 ◽  
Author(s):  
Erika Crouch ◽  
Nikolaos Nikolaidis ◽  
Francis X. McCormack ◽  
Barbara McDonald ◽  
Kimberly Allen ◽  
...  
Keyword(s):  
Influenza A ◽  
Surfactant Protein ◽  
Surfactant Protein D ◽  
X Ray ◽  
X Ray Crystallography

Circulating Surfactant Protein D Is Decreased in Systemic Lupus Erythematosus

2009 ◽  
Vol 36 (11) ◽  
pp. 2449-2453 ◽  
Author(s):  
SILJE VERMEDAL HOEGH ◽  
ANNE VOSS ◽  
GRITH LYKKE SORENSEN ◽  
ANETTE HØJ ◽  
CHRISTIAN BENDIXEN ◽  
...  
Keyword(s):  
Systemic Lupus Erythematosus ◽  
Lupus Erythematosus ◽  
Surfactant Protein ◽  
Innate Immune ◽  
Surfactant Protein D ◽  
Systemic Lupus ◽  
Reactive Protein ◽  
Structural And Functional Properties ◽  
Disease Indicators ◽  
And Function

Objective.Deficiencies of innate immune molecules like mannan binding lectin (MBL) have been implicated in the pathogenesis of systemic lupus erythematosus (SLE). Surfactant protein D (SP-D) and MBL belong to the same family of innate immune molecules — the collectins, which share important structural and functional properties. We aimed to compare concentrations of serum SP-D in patients with SLE and in healthy controls, and to investigate if SP-D is associated with selected disease indicators. We investigated the possible association of the Met11Thr polymorphism with disease, since this polymorphism is an important determinant for serum level, oligomerization pattern, and function of SP-D.Methods.Serum SP-D was measured using a 5-layer ELISA in 70 SLE patients and 1476 healthy subjects. DNA was genotyped for the Met11Thr variant.Results.Median SP-D level in serum was 911 ng/ml (95% CI 776–1118) in patients and 1068 ng/ml (95% CI 901–1246) in controls (p = 0.0004). Circulating SP-D did not differ significantly in patients with high, intermediate, or low SLE disease activity. Similarly, SP-D did not correlate with C-reactive protein, erythrocyte sedimentation rate, and anti-dsDNA seropositivity. Genetic analysis did not support an association of the Met11Thr genotype with SLE.Conclusion.These findings suggest that low SP-D, unrelated to conventional disease indicators, represents an aspect of SLE etiopathogenesis.

Bovine conglutinin (BC) mRNA expressed in liver: cloning and characterization of the BC cDNA reveals strong homology to surfactant protein-D

Gene ◽  
1994 ◽  
Vol 141 (2) ◽  
pp. 277-281 ◽  
Author(s):  
Louis S Liou ◽  
Rajeswari Sastry ◽  
Kevan L Hartshorn ◽  
Young Moo Lee ◽  
Thomas B Okarma ◽  
...  
Keyword(s):  
Surfactant Protein ◽  
Surfactant Protein D ◽  
Strong Homology
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