<div class="csl-bib-body">
<div class="csl-entry">Garcia de Otazo Hernandez, D., Sabatino, G., Maliqi, C., Sgarz, P., Seltenhammer, I., Koidl, L., Rohrhofer, J., Keppler, S. J., Untersmayr, E., & Ret, D. (2026, March 3). <i>Erythrocyte desialylation and rheological consequences in PAIS patients</i> [Conference Presentation]. Connecting Minds - Scientific Symposium on PAIS, Wien, Austria. http://hdl.handle.net/20.500.12708/226857</div>
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dc.identifier.uri
http://hdl.handle.net/20.500.12708/226857
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dc.description.abstract
Background
Erythrocytes and the apical surface of vascular endothelial cells are covered by a dense sheet of glycans termed the glycocalyx. It is composed of a negatively charged network of proteoglycans, glycoproteins, and glycolipids. The negative charge is afforded and maintained through heavy sialylation and sulfation. In our previous study a significantly higher amount of free sialic acid was detected in blood serum from patients suffering of post-acute infectious syndromes (PAIS). It is known that neuraminidase-mediated cleavage of sialic acid from erythrocytes leads to increased lactate formation, cell shape alteration and enhanced mononuclear phagocytic clearance [1]. In our study we aim to evaluate erythrocyte glycocalyx damage leading to decreased surface charge, which can result in impaired microcirculation and O2-delivery in patients suffering from PAIS.
Methods
Erythrocytes from ME/CFS patients were collected and used in hemagglutination assays with sialic acid-specific lectin SNA (S. nigra). These were compared with healthy controls. N-glycan analysis of healthy erythrocyte membranes was performed. N-glycans were separated and relatively quantified using HPLC-FL and assigned based on MALDI mass spectrometry data. Rheology measurements were conducted of intact and neuraminidase-induced de-sialylated erythrocytes.
Results
Erythrocytes isolated from ME/CFS patients demonstrated significantly reduced hemagglutination compared to those from healthy controls. This finding is consistent with previous reports of elevated free sialic acid levels in serum and may indicate increased shedding of sialic acid from the erythrocyte surface. Analysis of surface-bound N-glycans revealed that di- and mono-sialylated glycan species were the predominant structures detected. Distinct rheological behaviors were observed between intact and desialylated erythrocytes. Specifically, in vitro neuraminidase treatment resulted in a marked reduction in erythrocyte flexibility, likely attributable to altered surface charge and membrane-associated properties.
Conclusion
The results point to a loss of sialic acid on erythrocytes from patients with disease. The resulting damage may cause a reduction of erythrocyte flexibility which negatively influences vascular capillary flow. N-glycan analysis of erythrocyte membranes from ME/CFS-affected individuals can be a useful method to accurately gauge the degree of surface sialic acid loss.
en
dc.description.sponsorship
WWTF Wiener Wissenschafts-, Forschu und Technologiefonds
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dc.language.iso
en
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dc.subject
ME/CFS
en
dc.subject
Blood
en
dc.subject
Sialic acid
en
dc.subject
Rheology
en
dc.subject
Long COVID
en
dc.subject
Hemodynamics
en
dc.subject
Glycosylation
en
dc.title
Erythrocyte desialylation and rheological consequences in PAIS patients
en
dc.type
Presentation
en
dc.type
Vortrag
de
dc.contributor.affiliation
TU Wien, Austria
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dc.contributor.affiliation
TU Wien, Austria
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dc.contributor.affiliation
Medical University of Vienna, Austria
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dc.contributor.affiliation
Medical University of Graz, Austria
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dc.contributor.affiliation
Medical University of Vienna, Austria
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dc.relation.grantno
ME-CFS24-016
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dc.type.category
Conference Presentation
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tuw.publication.invited
invited
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tuw.project.title
Exploring the Glycome: Identifying Glycosylation-Related Biomarkers in Chronic Fatigue Syndrome
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tuw.researchTopic.id
M1
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tuw.researchTopic.id
M6
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tuw.researchTopic.id
X1
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tuw.researchTopic.name
Surfaces and Interfaces
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tuw.researchTopic.name
Biological and Bioactive Materials
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tuw.researchTopic.name
Beyond TUW-research focus
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tuw.researchTopic.value
40
-
tuw.researchTopic.value
50
-
tuw.researchTopic.value
10
-
tuw.publication.orgunit
E163-02-1 - Forschungsgruppe Polymerchemie und Technologie
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tuw.author.orcid
0000-0003-0126-3868
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tuw.author.orcid
0009-0004-5807-5870
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tuw.author.orcid
0009-0005-8573-1930
-
tuw.author.orcid
0009-0002-8488-0481
-
tuw.author.orcid
0009-0009-4310-4962
-
tuw.author.orcid
0000-0001-9974-7929
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tuw.author.orcid
0000-0002-2783-2099
-
tuw.author.orcid
0000-0002-9010-8044
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tuw.author.orcid
0000-0002-1963-499X
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tuw.author.orcid
0000-0002-7461-0923
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tuw.event.name
Connecting Minds - Scientific Symposium on PAIS
en
tuw.event.startdate
03-03-2026
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tuw.event.enddate
03-03-2026
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tuw.event.online
Hybrid
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tuw.event.type
Event for scientific audience
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tuw.event.place
Wien
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tuw.event.country
AT
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tuw.event.institution
National Reference Center for Post-Viral Syndromes
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tuw.event.presenter
Garcia de Otazo Hernandez, Daniel
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tuw.presentation.online
Online
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tuw.event.track
Single Track
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wb.sciencebranch
Chemie
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wb.sciencebranch
Medizinische Biochemie, Humangenetik
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wb.sciencebranch
Anatomie, Pathologie, Physiologie
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wb.sciencebranch.oefos
1040
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wb.sciencebranch.oefos
3013
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wb.sciencebranch.oefos
3011
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wb.sciencebranch.value
30
-
wb.sciencebranch.value
40
-
wb.sciencebranch.value
30
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item.openairecristype
http://purl.org/coar/resource_type/c_18cp
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item.grantfulltext
restricted
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item.cerifentitytype
Publications
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item.openairetype
conference paper not in proceedings
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item.languageiso639-1
en
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item.fulltext
no Fulltext
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crisitem.author.dept
TU Wien, Austria
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crisitem.author.dept
TU Wien, Austria
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crisitem.author.dept
E163-02-1 - Forschungsgruppe Polymerchemie und Technologie
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crisitem.author.dept
Medical University of Vienna, Austria
-
crisitem.author.dept
Medical University of Graz, Austria
-
crisitem.author.dept
Medical University of Vienna, Austria
-
crisitem.author.dept
E163-02-1 - Forschungsgruppe Polymerchemie und Technologie
