Evidence map›Paper›PMID 40730944›Full record

ArticleBMC microbiology2025

Agglutination of yeast-binding antibodies from human blood plasma products.

Robbi Miguel G Falcon, Fresthel Monica M Climacosa, Salvador Eugenio C Caoili

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Article in BMC microbiology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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1 · What the graph read from it

What it found

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2 · The registry

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3 · Its place in the literature

Who cites it

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4 · The record

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5 · Who and what money

Authors and funding

3 authors.

Robbi Miguel G FalconBiomedical Innovations Research for Translational Health Science (BIRTHS) Laboratory, Department of Biochemistry and Molecular Biology, College of Medicine, University of the Philippines Manila, Manila, Philippines. rgfalcon@up.edu.ph.
Fresthel Monica M ClimacosaBiomedical Innovations Research for Translational Health Science (BIRTHS) Laboratory, Department of Biochemistry and Molecular Biology, College of Medicine, University of the Philippines Manila, Manila, Philippines.
Salvador Eugenio C CaoiliBiomedical Innovations Research for Translational Health Science (BIRTHS) Laboratory, Department of Biochemistry and Molecular Biology, College of Medicine, University of the Philippines Manila, Manila, Philippines.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundYeasts are ubiquitous microorganisms found both endogenously within the human body and in the environment. Humoral responses against yeasts lead to the production of yeast-binding antibodies, which can agglutinate yeast cell targets. These antibodies affect the accuracy of immunodiagnostic tools employing yeast cells as in recombinant surface antigen display.

aimTo improve the applicability of such tools, the study aims to determine the abundance and characterize the agglutinating behavior of yeast-binding antibodies. METHODOLOGY: The study employed the use of a yeast agglutination assay to determine the prevalence of agglutination across human fresh frozen plasma samples (n = 36). The mean area of the agglutinin complex served as the basis for differentiating positive and negative samples. Indirect ELISA set-ups using protein A, protein G, and anti-IgM horseradish peroxidase conjugates were used to quantify titers and characterize the isotypes driving agglutination.

resultsThe results of the agglutination assays and indirect ELISA revealed that the formation of agglutinin complexes was promoted by a low pH and inhibited by a high ionic strength. Coagulation factors and complement proteins did not significantly contribute to agglutination. Finally, elution of agglutinating proteins was performed and the resulting eluate was tested further for re-binding and re-agglutination with yeast cells, suggesting the presence of antibodies.

conclusionFindings from the current study suggest that antibody-mediated yeast cell agglutination driven by immunoglobulins (i.e., IgM, IgG) present in human plasma can be affected by various physicochemical factors such as pH (i.e., acidity) and ionic strength (i.e., NaCl concentration) but is independent of the activity of coagulation factors. These conditions must be carefully optimized in the development of cell-based immunoassays and yeast surface display technologies, which utilize antibody-mediated yeast agglutination.

Indexed as

Antibodies, FungalPlasmaSaccharomyces cerevisiaeYeastsAgglutinationAgglutination TestsEnzyme-Linked Immunosorbent AssayHumansHydrogen-Ion ConcentrationAntibodies, FungalAgglutinationFresh frozen plasmaIgGIgMSaccharomyces cerevisiae

Identifiers

PMID40730944
PMCPMC12306107

What Socratic holds

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.