Repertoire of human natural anti-glycan immunoglobulins. Do we have auto-antibodies?

Bovin, Nicolai V.; Obukhova, Polina; Шилова, Н. В.; Rapoport, E. M.; Popova, I. S.; Navakouski, Maksim; Unverzagt, Carlo; Vuskovic, Marko; Huflejt, Margaret E.

doi:10.1016/j.bbagen.2012.02.005

Cited by 73 publications

(73 citation statements)

References 50 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Two of the structures on the array containing an internal LNnT determinant as part of a larger structure, #330 (Galα1-4Galβ1-4 GlcNAcβ1-3Galβ1-4Glcβ-) and #331 (GalNAcβ1-3Galα1-4Galβ1-4 GlcNAcβ1-3Galβ1-4Glcβ-) were found at low levels in one or two of the pre-bleed sera and were boosted in all three immunization groups, thus these antibodies were probably not a result of the specific immunogens. Antibodies to a few unrelated structures (#400, #304, 502) were also boosted in all three groups; these could be natural antibodies that are boosted non-specifically by the immunization, and some of these specificities (#304; 330 – blood group P1 antigen) and antibodies to related antigens (#400, 331) have been previously reported in serum from healthy human donors 22 .…”

Section: Resultssupporting

confidence: 54%

“…Normal human serum and intravenous immunoglobulin (IVIG) derived from it have previously been shown to contain antibodies that recognize many self-like determinants, including LNnT and LNT 22,24,25 . Interestingly, and by contrast, we did not detect such antibodies to LNnT in naïve rabbit serum, although it did contain antibodies to several of the CFG glycan determinants, and recognition against them was boosted after our immunization.…”

Section: Discussionmentioning

confidence: 99%

“…Lac-OR-AEAB, LNnT-OR-AEAB and LNnT-CR-AEAB were prepared as described [22] and the glycoprotein conjugates described above were printed in hexareplicate spots on NHS-activated glass slides (Schott, Tempe, AZ) using a Piezo Printer (Piezorray, PerkinElmer). Derivatized glycans were printed with 2 drops (666pL) of 100μM solutions and glycoproteins were printed with 2 drops of 0.5mg/mL solutions, in phosphate buffer, pH 8.0.…”

Section: Methodsmentioning

confidence: 99%

See 2 more Smart Citations

Intact Reducing Glycan Promotes the Specific Immune Response to Lacto-N-neotetraose-BSA Neoglycoconjugates

et al. 2015

View full text Add to dashboard Cite

The mammalian immune system responds to eukaryotic glycan antigens during infections, cancer, and autoimmune disorders, but the immunological bases for such responses are unclear. Conjugate vaccines containing bacterial polysaccharides linked to carrier proteins (neoglycoconjugates) have proven successful, but these often contain repeating epitopes and the reducing end of the glycan is less important, unlike typical glycan determinants in eukaryotes, which are shorter in length and may include the reducing end. Here we have compared the effects of two linkage methods, one that opens the ring at the reducing end of the glycan, and one that leaves the reducing end closed, on the glycan specificity of the vaccine response in rabbits and mice. We immunized rabbits and mice with bovine serum albumin (BSA) conjugates of synthetic open- and closed-ring forms (OR versus CR) of a simple tetrasaccharide lacto-N-neo-tetraose (LNnT, Galβ1-4GlcNAcβ1-3Galβ1-4Glc), and tested reactivity to the immunogens and several related glycans in both OR and CR versions on glycan microarrays. We found that in rabbits the immune response to the CR conjugate was directed toward the glycan, whereas the OR conjugate elicited antibodies to the reducing end of the glycan and linker region but not specifically to the glycan itself. Unexpectedly, mice did not generate a glycan-specific response to the CR conjugate. Our findings indicate that the reducing end of the sugar is crucial for generation of a glycan-specific response to some eukaryotic vaccine epitopes, and that there are species-specific differences in the ability to make a glycan-specific response to some glycoconjugates. These findings warrant further investigation with regard to rational design of glycoconjugate vaccines.

show abstract

Section: Resultssupporting

confidence: 54%

Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

See 1 more Smart Citation

Intact Reducing Glycan Promotes the Specific Immune Response to Lacto-N-neotetraose-BSA Neoglycoconjugates

et al. 2015

View full text Add to dashboard Cite

show abstract

“…Additional possible MM biomarkers have been reported in the recent literature [41,42,43], and are awaiting further evaluation and validation for clinical practice. Hyaluronan is a glycosaminoglycan often secreted in large amounts into MM effusions: a concentration exceeding 250 g/l is only seen in MM effusions [40,44] and appears to be specific for this diagnosis, but such high levels are only obtained in 50-60% of MM effusions.…”

Section: Optional Ancillary Techniquesmentioning

confidence: 99%

Guidelines for the Cytopathologic Diagnosis of Epithelioid and Mixed-Type Malignant Mesothelioma

et al. 2015

View full text Add to dashboard Cite

Objective: To provide practical guidelines for the cytopathologic diagnosis of malignant mesothelioma. Data Sources: Cytopathologists with an interest in the field involved in the International Mesothelioma Interest Group (IMIG) and the International Academy of Cytology (IAC) contributed to this update. Reference material includes peer-reviewed publications and textbooks. Rationale: This article is the result of discussions during and after the IMIG 2012 conference in Boston, followed by thorough discussions during the 2013 IAC meeting in Paris. Additional contributions have been obtained from cytopathologists and scientists who could not attend these meetings, with final discussions and input during the IMIG 2014 conference in Cape Town.

show abstract

“…Stejně jako je dnes jasné, že v sé-rech pacientů s rakovinou jsou přítomny protilátky, které se mohou vázat ke glykanům a ně kte rým glykoproteinům [18], pak i detekce anti-rakovinných glykokonjugátových protilátek v sérech pacientů může být v budoucnosti důležitá pro dia gnostické a prognostické metody. Populární aplikací těchto principů jsou glykanové čipy [19,20], o kterých bude pojednáno později.…”

Section: S123unclassified

New Trends in the Study of Protein Glycosylation in Oncological Diseases

Zahradníková¹,

Hernychová²,

Vojtěšek³

et al. 2014

Klin Onkol

View full text Add to dashboard Cite

Regionální centrum aplikované molekulární onkologie, Masarykův onkologický ústav, Brno SouhrnGlykomika a glykoproteomika představují relativně nové směry pro analýzy komplexních biologických vzorků a jejich důležitost neustále roste. Tyto oblasti jsou komplementární k dalším zavedeným přístupům, např. ke genomickému profi lování a proteomice. Glykoproteiny jsou stále více uznávány jako důležité molekuly účastnící se buněčných interakcí a adhezí. Výskyt strukturních změn v glykanových částech se zdá být typický pro různé typy rakoviny. Násle-dující souhrn se zabývá aktuálními trendy v glykomickém profi lování a glykoproteomickém výzkumu bio logických tekutin a tkání se zaměřením na rakovinu. Použité metody jsou založeny na principech kapilárních separačních technik, hmotnostní spektrometrie a glykanových a lektinových čipů. Všechny zmíněné metody mají značný potenciál pro využití v dia gnostických a prediktivních vyšetřeních. Klíčová slovaglykomika -glykopeptidy -rakovina -kapalinová chromatografi e -hmotnostní spektrometrie -kapilární elektroforéza -glykanové profi lování -čipové analýzy SummaryGlycomics and glycoproteomics represent relatively new directions in detail analyses of complex bio logical media. These areas of increasing importance to cancer research complement the more established genomic profi ling and proteomics. Glycoproteins are being increasingly recognized as important in cellular interactions and adhesion. Structural alterations of their glycan moieties seem to occur in diff erent cancer conditions. We review current directions in glycomic profi ling and glycoproteomic investigations of bio logical fl uids and tissues pertaining to cancer. The used methods rely on capillary separation techniques, mass spectrometry, and the glycan and lectin arrays. They all show considerable promise for new dia gnostic and prognostic measurements.

show abstract

Repertoire of human natural anti-glycan immunoglobulins. Do we have auto-antibodies?

Cited by 73 publications

References 50 publications

Intact Reducing Glycan Promotes the Specific Immune Response to Lacto-N-neotetraose-BSA Neoglycoconjugates

Intact Reducing Glycan Promotes the Specific Immune Response to Lacto-N-neotetraose-BSA Neoglycoconjugates

Guidelines for the Cytopathologic Diagnosis of Epithelioid and Mixed-Type Malignant Mesothelioma

New Trends in the Study of Protein Glycosylation in Oncological Diseases

Contact Info

Product

Resources

About