Solid-Phase Chemical Modification for Sialic Acid Linkage Analysis: Application to Glycoproteins of Host Cells Used in Influenza Virus Propagation

ABSTRACT Although sialic acid has long been recognized as the primary receptor determinant for attachment of influenza virus to host cells, the specific receptor molecules that mediate viral entry are not known for any cell type. For the infection of murine macrophages by influenza virus, our earlier study indicated involvement of a C-type lectin, the macrophage mannose receptor (MMR), in this process. Here, we have used direct binding techniques to confirm and characterize the interaction of influenza virus with the MMR and to seek additional macrophage surface molecules that may have potential as receptors for viral entry. We identified the macrophage galactose-type lectin (MGL) as a second macrophage membrane C-type lectin that binds influenza virus and is known to be endocytic. Binding of influenza virus to MMR and MGL occurred independently of sialic acid through Ca2+-dependent recognition of viral glycans by the carbohydrate recognition domains of the two lectins; influenza virus also bound to the sialic acid on the MMR. Multivalent ligands of the MMR and MGL inhibited influenza virus infection of macrophages in a manner that correlated with expression of these receptors on different macrophage populations. Influenza virus strain A/PR/8/34, which is poorly glycosylated and infects macrophages poorly, was not recognized by the C-type lectin activity of either the MMR or the MGL. We conclude that lectin-mediated interactions of influenza virus with the MMR or the MGL are required for the endocytic uptake of the virus into macrophages, and these lectins can thus be considered secondary or coreceptors with sialic acid for infection of this cell type.

Download Full-text

Identification of Amino Acid Residues in BK Virus VP1 That Are Critical for Viability and Growth

Journal of Virology ◽

10.1128/jvi.01316-07 ◽

2007 ◽

Vol 81 (21) ◽

pp. 11798-11808 ◽

Cited By ~ 39

Author(s):

Aisling S. Dugan ◽

Megan L. Gasparovic ◽

Natia Tsomaia ◽

Dale F. Mierke ◽

Bethany A. O'Hara ◽

...

Keyword(s):

Amino Acids ◽

Sialic Acid ◽

Burst Size ◽

Point Mutations ◽

Bk Virus ◽

Host Cells ◽

Wild Type Virus ◽

Wild Type ◽

Virion Protein ◽

Virus Propagation

ABSTRACT BK virus (BKV) is a ubiquitous pathogen that establishes a persistent infection in the urinary tract of 80% of the human population. Like other polyomaviruses, the major capsid protein of BKV, virion protein 1 (VP1), is critical for host cell receptor recognition and for proper virion assembly. BKV uses a carbohydrate complex containing α(2,3)-linked sialic acid attached to glycoprotein and glycolipid motifs as a cellular receptor. To determine the amino acids important for BKV binding to the sialic acid portion of the complex, we generated a series of 17 point mutations in VP1 and scored them for viral growth. The first set of mutants behaved identically to wild-type virus, suggesting that these amino acids were not critical for virus propagation. Another group of VP1 mutants rendered the virus nonviable. These mutations failed to protect viral DNA from DNase I digestion, indicating a role for these domains in capsid assembly and/or packaging of DNA. A third group of VP1 mutations packaged DNA similarly to the wild type but failed to propagate. The initial burst size of these mutations was similar to that of the wild type, indicating that there is no defect in the lytic release of the mutated virions. Binding experiments revealed that a subset of the BKV mutants were unable to attach to their host cells. These motifs are likely important for sialic acid recognition. We next mapped these mutations onto a model of BKV VP1 to provide atomic insight into the role of these sites in the binding of sialic acid to VP1.

Download Full-text

Effect of solid-phase chemical modification on the features of the lipase from Thermomyces lanuginosus

Process Biochemistry ◽

10.1016/j.procbio.2011.12.001 ◽

2012 ◽

Vol 47 (3) ◽

pp. 460-466 ◽

Cited By ~ 26

Author(s):

Magaly Galvis ◽

Oveimar Barbosa ◽

Rodrigo Torres ◽

Claudia Ortiz ◽

Roberto Fernandez-Lafuente

Keyword(s):

Chemical Modification ◽

Solid Phase ◽

Thermomyces Lanuginosus ◽

Phase Chemical

Download Full-text

Interfacial Solid-Phase Chemical Modification with Mannich Reaction and Fe(III) Chelation for Designing Lignin-Based Spherical Nanoparticle Adsorbents for Highly Efficient Removal of Low Concentration Phosphate from Water

ACS Sustainable Chemistry & Engineering ◽

10.1021/acssuschemeng.7b00674 ◽

2017 ◽

Vol 5 (8) ◽

pp. 6539-6547 ◽

Cited By ~ 32

Author(s):

Xiaogang Luo ◽

Chao Liu ◽

Jun Yuan ◽

Xingrong Zhu ◽

Shilin Liu

Keyword(s):

Chemical Modification ◽

Mannich Reaction ◽

Solid Phase ◽

Efficient Removal ◽

Low Concentration ◽

Highly Efficient ◽

Phase Chemical

Download Full-text

Tuning of Lecitase features via solid-phase chemical modification: Effect of the immobilization protocol

Process Biochemistry ◽

10.1016/j.procbio.2014.01.028 ◽

2014 ◽

Vol 49 (4) ◽

pp. 604-616 ◽

Cited By ~ 43

Author(s):

Cristina Garcia-Galan ◽

José C.S. dos Santos ◽

Oveimar Barbosa ◽

Rodrigo Torres ◽

Ernandes B. Pereira ◽

...

Keyword(s):

Chemical Modification ◽

Solid Phase ◽

Modification Effect ◽

Phase Chemical

Download Full-text

Sialic Acid Linkage Analysis Refines the Diagnosis of Ovarian Cancer

Frontiers in Oncology ◽

10.3389/fonc.2019.00261 ◽

2019 ◽

Vol 9 ◽

Cited By ~ 12

Author(s):

Tereza Dědová ◽

Elena Iona Braicu ◽

Jalid Sehouli ◽

Véronique Blanchard

Keyword(s):

Ovarian Cancer ◽

Sialic Acid ◽

Linkage Analysis ◽

Sialic Acid Linkage

Download Full-text

Tissue distribution of human and avian type sialic acid influenza virus receptors in domestic cat

Acta Veterinaria Hungarica ◽

10.1556/avet.2013.030 ◽

2013 ◽

Vol 61 (4) ◽

pp. 537-546 ◽

Cited By ~ 11

Author(s):

Heng Wang ◽

Xintao Wu ◽

Yanfen Cheng ◽

Yufu An ◽

Zhangyong Ning

Keyword(s):

Influenza Virus ◽

Sialic Acid ◽

Gastrointestinal Tract ◽

Virus Infection ◽

Tissue Distribution ◽

Influenza Virus Infection ◽

Influenza Viruses ◽

Domestic Cat ◽

Host Cells ◽

Human Influenza

Infection of host cells with the influenza virus is mediated by specific interactions between the viral haemagglutinin (HA) and cell oligosaccharides containing sialic acid (SA) residues. Avian and human influenza viruses bind to alpha-2, 3 and alpha-2, 6 sialic acid-linked receptors, respectively. To date, there have been no detailed tissue distribution data on alpha-2, 3 and alpha-2, 6 sialic acid-linked receptors in the domestic cat, a relatively new mammalian host for influenza virus infections. In this study, the tissue distribution of human and avian type sialic acid influenza receptors was determined in various organs (respiratory tract, gastrointestinal tract, brain, cerebellum, spleen, kidney, heart and pancreas) of domestic cat by binding with the lectinsMaackia amurensisagglutinin II (MAA II) andSambucus nigraagglutinin (SNA), respectively. The results revealed that both alpha-2, 3 and alpha-2, 6 sialic acid-linked receptors were extensively detected in the trachea, bronchus, lung, kidney, spleen, pancreas and gastrointestinal tract. Endothelial cells of gastrointestinal tract organs were negative for alpha-2, 3 sialic acid-linked receptors in cats. The presence of alpha-2, 3 and alpha-2, 6 sialic acid-linked receptors in the major organs examined in the present study suggests that each major organ may be affected by influenza virus infection. Because of receptor distribution in the gastrointestinal tract, the experimental infection of cats with human influenza virus may be relatively easy while their infection with avian influenza virus may be difficult. These data can explain the involvement of multiple organs in influenza virus infection and should help investigators interpret the results obtained when cats are infected with influenza virus and estimate the risk of infection between cats and humans.

Download Full-text

Sialic Acid-Binding Immunoglobulin-Like Lectin 7 Mediates Selective Recognition of Sialylated Glycans Expressed on Campylobacter jejuni Lipooligosaccharides

Infection and Immunity ◽

10.1128/iai.02094-05 ◽

2006 ◽

Vol 74 (7) ◽

pp. 4133-4141 ◽

Cited By ~ 89

Author(s):

Tony Avril ◽

Eric R. Wagner ◽

Hugh J. Willison ◽

Paul R. Crocker

Keyword(s):

Sialic Acid ◽

Campylobacter Jejuni ◽

Solid Phase ◽

Specific Binding ◽

Chinese Hamster Ovary Cells ◽

Chinese Hamster ◽

Host Cells ◽

Blood Leukocytes ◽

Ovary Cells ◽

Sialic Acid Binding

ABSTRACT siglecs are a family of sialic-acid binding immunoglobulin-like lectins mostly expressed by cells of the immune system that have the potential to interact with sialylated glycans expressed not only on host cells but also on certain pathogens. Campylobacter jejuni is a common pathogen of humans that expresses surface lipooligosaccharides (LOS) that can be modified with ganglioside-like terminal structures in the core oligosaccharides. In this study, we examined the interaction of 10 siglecs with LOS purified from four different C. jejuni isolates expressing GM1-like, GD1a-like, GD3-like, and GT1a-like oligosaccharides. Of all siglecs examined, only Siglec-7 exhibited specific, sialic acid-dependent interactions with C. jejuni LOS in solid-phase binding assays. Binding was especially prominent with LOS from the HS:19(GM1+ GT1a+) isolate, with weaker binding with LOS from the HS:19(GD3+) isolate. Binding of Siglec-7 was also observed with intact bacteria expressing these LOS structures. Specific binding of HS:19(GM1+ GT1a+) bacteria was demonstrated with Siglec-7 expressed on transfected Chinese hamster ovary cells and with peripheral blood leukocytes, among which HS:19(GM1+ GT1a+) bacteria bound selectively to both natural killer cells and monocytes which naturally express Siglec-7. These results raise the possibility that, in addition to their role in generating autoimmune antibody responses, C. jejuni LOS could interact with Siglec-7 expressed by leukocytes, modulate the host-pathogen interaction, and contribute to the clinical outcome and the development of secondary complications such as Guillain-Barré syndrome.

Download Full-text