scholarly journals Sialic acid receptors: focus on their role in influenza infection

2018 ◽  
Vol Volume 10 ◽  
pp. 1-11 ◽  
Author(s):  
Guadalupe Ayora-Talavera
Keyword(s):  
Sialic Acid ◽  
Influenza Infection ◽  
Sialic Acid Receptors

#10: Tropism, Susceptibility, and Infectivity of Differentiated Human Tonsillar Epithelial Cells by Different Influenza Viruses

2021 ◽  
Vol 10 (Supplement_2) ◽  
pp. S7-S7
Author(s):  
Faten A Okda* ◽  
Richard Webby
Keyword(s):  
Influenza Virus ◽  
Sialic Acid ◽  
Epithelial Cells ◽  
Influenza A ◽  
Influenza Infection ◽  
Influenza Viruses ◽  
H3n2 Virus ◽  
Ciliated Cells ◽  
Human Tonsil ◽  
Sialic Acid Receptors

Abstract Introduction Influenza viruses cause significant socioeconomic impact due to annual outbreaks and pandemic risks. Human tonsil epithelium cells (HTEC) are a heterogeneous group of actively differentiating epithelia comprising stratified squamous epithelium and reticulated crypt cells with abundant keratin expression. Hypothesis We hypothesized that the tonsils are a primary site for influenza infection and sustained viral replication. Methods and Results Primary HTEC (ScienCell Research Laboratories) were grown using an air-liquid interface and infected apically with different influenza viruses at various MOIs to measure viral growth kinetics. These cells were highly differentiated, with subpopulations of cells including ciliated, non-ciliated cells and specialized cells with secretory functions. There was a heterogenous distribution of both human-like (α2,6-linked) and avian-like (α2,3-linked) sialic acid receptors. The HTEC surface and crypts were lined with pseudostratified columnar ciliated cells possessing both α2,6-linked and α2,3-linked sialic acid receptors that were interrupted by patches of reticular epithelial cells. The HTEC epithelial cells were permissive for growth of influenza A and B viruses. A subset of cells, mostly ciliated cells, underwent apoptosis while others including non-ciliated cells remained intact despite being positive for influenza virus nucleoprotein. Interestingly, differences were seen between subtypes with colocalization of H3N2 virus and non-ciliated cells while H1N1 virus mostly associated with ciliated cells. Conclusion Our results implicated human tonsillar crypt epithelium as a site for influenza virus replication. The tonsil epithelium cell culture differentiated system provides a valuable in vitro model for studying cellular tropism, infectivity, cytokines immune response and the pathogenesis of influenza viruses for better development of effective universal vaccine and therapies against different strains of influenza viruses.

Avian influenza and sialic acid receptors: more than meets the eye?

2005 ◽  
Vol 5 (3) ◽  
pp. 184-188 ◽  
Author(s):  
S OLOFSSON ◽  
U KUMLIN ◽  
K DIMOCK ◽  
N ARNBERG
Keyword(s):  
Sialic Acid ◽  
Avian Influenza ◽  
Sialic Acid Receptors

Recognition in Novel Molecularly Imprinted Polymer Sialic Acid Receptors in Aqueous Media

1996 ◽  
Vol 29 (7) ◽  
pp. 1099-1107 ◽  
Author(s):  
Akimitsu Kugimiya∗ ◽  
Toshifumi Takeuchi ◽  
Jun Matsuib ◽  
Kazunori Ikebukuro ◽  
Kazuyoshi Yano ◽  
...  
Keyword(s):  
Sialic Acid ◽  
Molecularly Imprinted Polymer ◽  
Aqueous Media ◽  
Imprinted Polymer ◽  
Molecularly Imprinted ◽  
Sialic Acid Receptors

scholarly journals Protein-bound sialic acid in saliva contributes directly to salivary anti-influenza virus activity

2021 ◽  
Author(s):  
Kaori Kobayashi ◽  
Chika Shono ◽  
Takuya Mori ◽  
Hidefumi Kitazawa ◽  
Noriyasu Ota ◽  
...  
Keyword(s):  
Sialic Acid ◽  
Influenza A ◽  
Significant Positive Correlation ◽  
Influenza Infection ◽  
Respiratory Viruses ◽  
Biological Factor ◽  
Virus Activity ◽  
Individual Variations ◽  
Antiviral Activities ◽  
Direct Regulator

ABSTRACTThe oral cavity is an entrance for respiratory viruses, such as influenza. Recently, saliva has been shown to exert both antimicrobial and antiviral activities. Thus, saliva may be a biological factor that contributes to the prevention of influenza infection. However, the actual salivary anti-influenza A virus (IAV) activity in individuals and its determinant factors are unknown. By assessing individual variations in salivary anti-IAV activity in 92 people using an established new high-throughput system in this study, we found that the anti-IAV activity varied widely between individuals and showed a significant positive correlation with protein-bound sialic acid (BSA) level (ρ=0.473; p < 0.001). Furthermore, the anti-IAV activity of saliva with enzymatically reduced BSA content was significantly lower. These results indicate that BSA is a direct regulator of salivary anti-IAV activity and is a determinant of individual differences. Additionally, after comparing the anti-IAV activity across the groups by age, anti-IAV activity in young people (aged 5–19 years) were lower than in adults aged 20–59 years and elderly people aged 60–79 years. Our study suggests that BSA levels in saliva may be important in preventing influenza infection.

scholarly journals Antiviral adhesion molecular mechanisms for influenza: W. G. Laver's lifetime obsession

2015 ◽  
Vol 370 (1661) ◽  
pp. 20140034 ◽  
Author(s):  
Elspeth F. Garman
Keyword(s):  
Sialic Acid ◽  
Host Cell ◽  
Molecular Mechanisms ◽  
Surface Protein ◽  
X Ray Crystallography ◽  
Sialic Acid Receptors ◽  
Sialic Acid Binding ◽  
Viral Surface Protein ◽  
Viral Surface

Infection by the influenza virus depends firstly on cell adhesion via the sialic-acid-binding viral surface protein, haemagglutinin, and secondly on the successful escape of progeny viruses from the host cell to enable the virus to spread to other cells. To achieve the latter, influenza uses another glycoprotein, the enzyme neuraminidase (NA), to cleave the sialic acid receptors from the surface of the original host cell. This paper traces the development of anti-influenza drugs, from the initial suggestion by MacFarlane Burnet in 1948 that an effective ‘competitive poison’ of the virus' NA might be useful in controlling infection by the virus, through to the determination of the structure of NA by X-ray crystallography and the realization of Burnet's idea with the design of NA inhibitors. A focus is the contribution of the late William Graeme Laver, FRS, to this research.

scholarly journals Combinatorial design of a sialic acid imprinted binding site exploring a dual ion receptor approach

RSC Advances ◽  
2021 ◽  
Vol 11 (54) ◽  
pp. 34329-34337
Author(s):  
Liliia Mavliutova ◽  
Elena Verduci ◽  
Börje Sellergren
Keyword(s):  
Sialic Acid ◽  
Crown Ether ◽  
Binding Site ◽  
Combinatorial Design ◽  
Sialic Acid Receptors ◽  
Ion Imprinting

Dual-ion imprinting of sialic acid via cooperatively acting ureido- and crown ether functionalities leads to charge neutral sialic acid receptors with strong sialoglycopeptide affinity.

scholarly journals Direct and label-free influenza virus detection based on multisite binding to sialic acid receptors

2017 ◽  
Vol 92 ◽  
pp. 234-240 ◽  
Author(s):  
Yukichi Horiguchi ◽  
Tatsuro Goda ◽  
Akira Matsumoto ◽  
Hiroaki Takeuchi ◽  
Shoji Yamaoka ◽  
...  
Keyword(s):  
Influenza Virus ◽  
Sialic Acid ◽  
Virus Detection ◽  
Label Free ◽  
Sialic Acid Receptors ◽  
Influenza Virus Detection

scholarly journals Role of Neuraminidase in Influenza A(H7N9) Virus Receptor Binding

2017 ◽  
Vol 91 (11) ◽  
Author(s):  
Donald J. Benton ◽  
Stephen A. Wharton ◽  
Stephen R. Martin ◽  
John W. McCauley
Keyword(s):  
Sialic Acid ◽  
Cell Surface ◽  
Binding Site ◽  
Influenza A Virus ◽  
Receptor Binding ◽  
Influenza A ◽  
Health Concern ◽  
H7n9 Virus ◽  
Virus Receptor ◽  
Sialic Acid Receptors

ABSTRACT Influenza A(H7N9) viruses have caused a large number of zoonotic infections since their emergence in 2013. They remain a public health concern due to the repeated high levels of infection with these viruses and their perceived pandemic potential. A major factor that determines influenza A virus fitness and therefore transmissibility is the interaction of the surface glycoproteins hemagglutinin (HA) and neuraminidase (NA) with the cell surface receptor sialic acid. Typically, the HA is responsible for binding to the sialic acid to allow virus internalization and the NA is a sialidase responsible for cleaving sialic acid to aid virus spread and release. N9 NA has previously been shown to have receptor binding properties mediated by a sialic acid binding site, termed the hemadsorption (Hb) site, which is discrete from the enzymatically active sialidase site. This study investigated the N9 NA from a zoonotic H7N9 virus strain in order to determine its possible role in virus receptor binding. We demonstrate that this N9 NA has an active Hb site which binds to sialic acid, which enhances overall virus binding to sialic acid receptor analogues. We also show that the N9 NA can also contribute to receptor binding due to unusual kinetic characteristics of the sialidase site which specifically enhance binding to human-like α2,6-linked sialic acid receptors. IMPORTANCE The interaction of influenza A virus glycoproteins with cell surface receptors is a major determinant of infectivity and therefore transmissibility. Understanding these interactions is important for understanding which factors are necessary to determine pandemic potential. Influenza A viruses generally mediate binding to cell surface sialic acid receptors via the hemagglutinin (HA) glycoprotein, with the neuraminidase (NA) glycoprotein being responsible for cleaving the receptor to allow virus release. Previous studies showed that the NA proteins of the N9 subtype can bind sialic acid via a separate binding site distinct from the sialidase active site. This study demonstrates for purified protein and virus that the NA of the zoonotic H7N9 viruses has a binding capacity via both the secondary binding site and unusual kinetic properties of the sialidase site which promote receptor binding via this site and which enhance binding to human-like receptors. This could have implications for understanding human-to-human transmission of these viruses.

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