Changes in sialic acid expression in the lung during intrauterine development of the human fetus

Černá, Andrea; Janega, Pavol; Martanovič, P; Lisy, Milan; Babál, Pavel

doi:10.1078/0065-1281-00669

Cited by 25 publications

(13 citation statements)

References 9 publications

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“…Plant lectins, SNA-I and MALII that have been used extensively to characterize the distribution of α2,6 and α2,3 SA respectively in tissue sections from humans, ferrets, and mice 5,8,10,11,16,35,46,47 . Staining of ferret tracheal tissue have shown that airway epithelial cells predominantly express α2,6 SA while the submucosal glands express both α2,3 and α2,6 SA.…”

Section: Resultsmentioning

confidence: 99%

Receptor specificity does not affect replication or virulence of the 2009 pandemic H1N1 influenza virus in mice and ferrets

et al. 2013

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Human influenza viruses predominantly bind α2,6 linked sialic acid (SA) while avian viruses bind α2,3 SA-containing complex glycans. Virulence and tissue tropism of influenza viruses have been ascribed to this binding preference. We generated 2009 pandemic H1N1 (pH1N1) viruses with either predominant α2,3 or α2,6 SA binding and evaluated these viruses in mice and ferrets. The α2,3 pH1N1 virus had similar virulence in mice and replicated to similar titers in the respiratory tract of mice and ferrets as the α2,6 and WT pH1N1 viruses. Immunohistochemical analysis determined that all viruses infected similar cell types in ferret lungs. There is increasing evidence that receptor specificity of influenza viruses is more complex than the binary model of α2,6 and α2,3 SA binding and our data suggest that influenza viruses use a wide range of SA moieties to infect host cells.

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Section: Resultsmentioning

confidence: 99%

Receptor specificity does not affect replication or virulence of the 2009 pandemic H1N1 influenza virus in mice and ferrets

et al. 2013

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“…This paradigm may lead to novel skin cancer treatments, and pave the way to treat other cancers with elevated PDPN expression levels including breast [20], [24], glioma [21], and oral cancer [25], [26]. However, as stated above, while PDPN served as the model target of this investigation, other receptors with α2,3-sialic acid residues are increased in melanoma and a variety of other cancers, and may also be targeted to some extent by MASL [10], [12]–[14], [42].…”

Section: Discussionmentioning

confidence: 99%

“…However, antibody therapy presents challenges in administration and toxicity [40], [41]. Since PDPN is modified by α2,3-sialic acid, it can be targeted by specific lectins [10], [12]–[14], [42].…”

Section: Introductionmentioning

confidence: 99%

Plant Lectin Can Target Receptors Containing Sialic Acid, Exemplified by Podoplanin, to Inhibit Transformed Cell Growth and Migration

et al. 2012

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Cancer is a leading cause of death of men and women worldwide. Tumor cell motility contributes to metastatic invasion that causes the vast majority of cancer deaths. Extracellular receptors modified by α2,3-sialic acids that promote this motility can serve as ideal chemotherapeutic targets. For example, the extracellular domain of the mucin receptor podoplanin (PDPN) is highly O-glycosylated with α2,3-sialic acid linked to galactose. PDPN is activated by endogenous ligands to induce tumor cell motility and metastasis. Dietary lectins that target proteins containing α2,3-sialic acid inhibit tumor cell growth. However, anti-cancer lectins that have been examined thus far target receptors that have not been identified. We report here that a lectin from the seeds of Maackia amurensis (MASL) with affinity for O-linked carbohydrate chains containing sialic acid targets PDPN to inhibit transformed cell growth and motility at nanomolar concentrations. Interestingly, the biological activity of this lectin survives gastrointestinal proteolysis and enters the cardiovascular system to inhibit melanoma cell growth, migration, and tumorigenesis. These studies demonstrate how lectins may be used to help develop dietary agents that target specific receptors to combat malignant cell growth.

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“…Type II pneumocytes are surfactant-producing, alveolar epithelial cells and progenitor cells of both type I and type II cells. This cell type has been shown to contain sialic acid in newborn human lung (22). Whether the availability of the receptor alone determined the site of H5N1 infection needs further investigation.…”

Section: Discussionmentioning

confidence: 99%

Influenza A H5N1 Replication Sites in Humans

Uiprasertkul

Puthavathana

Sangsiriwut

et al. 2005

Emerg. Infect. Dis.

238

231

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Tissue tropism and pathogenesis of influenza A virus subtype H5N1 disease in humans is not well defined. In mammalian experimental models, H5N1 influenza is a disseminated disease. However, limited previous data from human autopsies have not shown evidence of virus dissemination beyond the lung. We investigated a patient with fatal H5N1 influenza. Viral RNA was detected by reverse transcription–polymerase chain reaction in lung, intestine, and spleen tissues, but positive-stranded viral RNA indicating virus replication was confined to the lung and intestine. Viral antigen was detected in pneumocytes by immunohistochemical tests. Tumor necrosis factor-α mRNA was seen in lung tissue. In contrast to disseminated infection documented in other mammals and birds, H5N1 viral replication in humans may be restricted to the lung and intestine, and the major site of H5N1 viral replication in the lung is the pneumocyte.

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Changes in sialic acid expression in the lung during intrauterine development of the human fetus

Cited by 25 publications

References 9 publications

Receptor specificity does not affect replication or virulence of the 2009 pandemic H1N1 influenza virus in mice and ferrets

Receptor specificity does not affect replication or virulence of the 2009 pandemic H1N1 influenza virus in mice and ferrets

Plant Lectin Can Target Receptors Containing Sialic Acid, Exemplified by Podoplanin, to Inhibit Transformed Cell Growth and Migration

Influenza A H5N1 Replication Sites in Humans

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