This article contains data related to the researc.h article entitled  Yeast-derived ArtinM shares structure, carbohydrate recognition, and biological effects with native ArtinM  by Cecílio et al. (2015) [1]. ArtinM, a D-mannose-binding lectin isolated from the seeds of Artocarpus heterophyllus, exerts immunomodulatory and regenerative activities through its Carbohydrate Recognition Domain (CRD) (Souza et al., 2013; Mariano et al., 2014 [2], [3]). The limited availability of the native lectin (n-ArtinM) led us to characterize a recombinant form of the protein, obtained by expression in Saccharomyces cerevisiae (y-ArtinM). We compared the carbohydrate-binding specificities of y-ArtinM and n-ArtinM by analyzing the binding of biotinylated preparations of the two lectin forms using a neoglycolipid (NGL)-based glycan microarray. Data showed that y-ArtinM mirrored the specificity exhibited by n-ArtinM

Carvalho, FC

Cecilio, NT

Feizi, T

Liu, Y

Roque Barreira, MC

Data in Brief

English

PubMed

AbstractThis article contains data related to the researc.h article entitled “Yeast-derived ArtinM shares structure, carbohydrate recognition, and biological effects with native ArtinM” by Cecílio et al. (2015) [1]. ArtinM, a D-mannose-binding lectin isolated from the seeds of Artocarpus heterophyllus, exerts immunomodulatory and regenerative activities through its Carbohydrate Recognition Domain (CRD) (Souza et al., 2013; Mariano et al., 2014 [2,3]). The limited availability of the native lectin (n-ArtinM) led us to characterize a recombinant form of the protein, obtained by expression in Saccharomyces cerevisiae (y-ArtinM). We compared the carbohydrate-binding specificities of y-ArtinM and n-ArtinM by analyzing the binding of biotinylated preparations of the two lectin forms using a neoglycolipid (NGL)-based glycan microarray. Data showed that y-ArtinM mirrored the specificity exhibited by n-ArtinM

Liu, Y.

Cecílio, N.T.

Carvalho, F.C.

Roque-Barreira, M.C.

Feizi, T.

Elsevier - Publisher Connector 

Contents lists available at ScienceDirect
Data in Brief
Data in Brief 5 (2015) 1035–1047http://d
2352-34
(http://c
DOI
n Corr
E-mjournal homepage: www.elsevier.com/locate/dibData ArticleGlycan microarray analysis of the
carbohydrate-recognition speciﬁcity of native
and recombinant forms of the lectin ArtinMY. Liu a,n, N.T. Cecílio b, F.C. Carvalho b, M.C. Roque-Barreira b,n,
T. Feizi a
a Glycosciences Laboratory, Department of Medicine, Imperial College London, London, United Kingdom
b Departamento de Biologia Celular e Molecular e Bioagentes Patogênicos, Faculdade de Medicina de Ribeirão
Preto, Universidade de São Paulo, Brazila r t i c l e i n f o
Article history:
Received 8 October 2015
Received in revised form
6 November 2015
Accepted 8 November 2015
Available online 18 November 2015
Keywords:
Glycan microarray
Lectin
ArtinM
Artocarpus heterophyllus
Immunomodulationx.doi.org/10.1016/j.dib.2015.11.014
09/& 2015 The Authors. Published by Else
reativecommons.org/licenses/by/4.0/).
of original article: http://dx.doi.org/10.1016
esponding authors.
ail addresses: yan.liu2@imperial.ac.uk (Y. Lia b s t r a c t
This article contains data related to the researc.h article entitled
“Yeast-derived ArtinM shares structure, carbohydrate recognition,
and biological effects with native ArtinM” by Cecílio et al. (2015)
[1]. ArtinM, a D-mannose-binding lectin isolated from the seeds of
Artocarpus heterophyllus, exerts immunomodulatory and regen-
erative activities through its Carbohydrate Recognition Domain
(CRD) (Souza et al., 2013; Mariano et al., 2014 [2,3]). The limited
availability of the native lectin (n-ArtinM) led us to characterize a
recombinant form of the protein, obtained by expression in Sac-
charomyces cerevisiae (y-ArtinM). We compared the carbohydrate-
binding speciﬁcities of y-ArtinM and n-ArtinM by analyzing the
binding of biotinylated preparations of the two lectin forms using a
neoglycolipid (NGL)-based glycan microarray. Data showed that
y-ArtinM mirrored the speciﬁcity exhibited by n-ArtinM.
& 2015 The Authors. Published by Elsevier Inc. This is an open
access article under the CC BY license
(http://creativecommons.org/licenses/by/4.0/).vier Inc. This is an open access article under the CC BY license
/j.ijbiomac.2015.09.062
u), mcrbarre@fmrp.usp.br (M.C. Roque-Barreira).
Y. Liu et al. / Data in Brief 5 (2015) 1035–10471036Speciﬁcation TableS
M
T
H
D
E
E
D
Dubject area Biology
ore speciﬁc sub-
ject areaGlycobiologyype of data Graphs and table
ow data was
acquiredThe data were generated from a NGL-based microarray system [4]. After
binding analyses, the slide was scanned using ProScanArray microarray
scanner (PerkinElmer) and the image ﬁles were quantiﬁed using ScanArray
Express software (PerkinElmer).ata format A dedicated in-house-designed software suite was used for storing, retriev-
ing and displaying carbohydrate microarray data [5], here as histogram
charts (Fig. 1) and result table (Table 1).xperimental
factorsn-ArtinM and y-ArtinM forms were biotinylated and analyzed for binding
using a NGL-based microarray (in-house designation ‘Array Sets 18–22bis’)
containing 255 lipid-linked glycan probes (Table 1).xperimental
featuresGlycan microarray analyses of an immunomodulatory lectinata source
locationUniversity of Sao Paulo, Brazil and Imperial College London, UK.ata accessibility The data are supplied with this article and will be online available at the Web
Portal of Glycosciences Laboratory, Imperial College London: https://gly
cosciences.med.ic.ac.uk/data.html.Value of the data
 The wide spectrum of glycans that constitute the glycan microarray makes this platform suitable to
compare the carbohydrate-binding speciﬁcities exhibited by native and recombinant lectins.
 The data derived from the NGL-based microarray analyses provide important information on the
carbohydrate binding speciﬁcities of y-ArtinM and n-ArtinM, and serve as the basis for further
studies on the ﬁne speciﬁcities of the lectins using other microarray systems or complementary
techniques.1. Data
In this study, we analyzed the native form of ArtinM and its yeast-derived counterpart, in terms of
their ability to bind to 255 glycans distributed in a microarray platform, in order to identify whether
n-ArtinM and y-ArtinM shared sugar-recognition speciﬁcity. Measurement of ﬂuorescence intensity
indicated that both preparations bound to N-glycan-related sequences (Fig. 1A and B), with a pre-
ference for probes having the core trimannoside Manα1-3(Manα1-6) Man. This binding intensity was
enhanced when the probe contained a Fucose residue at the trimannoside core (Table 1 – probe 131);
whereas binding was diminished when a similar position in the glycan was occupied by β1-2-linked
xylose (probes 130 and 132). Some differences between the two lectin forms were identiﬁed in the
magnitude of binding to probes 129, 131, 133, 135, 147, 148, 149, 150, 152, 153, 158, 159 and 160. In
general, y-ArtinM showed higher ﬂuorescence intensity than n-ArtinM.
Fig. 1. Carbohydrate microarray analyses of n-ArtinM (A) and y-ArtinM (B). Numerical scores of the binding signals are means
of duplicate spots at 7 fmol/spot (with error bars). The complete list of probes and their sequences and binding scores are in
Table 1.
Y. Liu et al. / Data in Brief 5 (2015) 1035–1047 10372. Materials and methods and data
2.1. Sample preparation
n-ArtinM was obtained from a saline extract of Artocarpus heterophyllus (jackfruit) seeds [6].
Saccharomyces cerevisiae BJ3501 was used to express y-ArtinM and the lectin was obtained by yeast
lysis [1]. n-ArtinM and y-ArtinM were puriﬁed by afﬁnity chromatography on a D-mannose column
Table 1
Oligosaccharide probes included in the microarray and the binding signals (means of the ﬂuorescence intensity at 7 fmol/probe
spot) of n-ArtinM and y-ArtinM.
Y. Liu et al. / Data in Brief 5 (2015) 1035–10471038
Table 1 (continued )
Y. Liu et al. / Data in Brief 5 (2015) 1035–1047 1039
Table 1 (continued )
Y. Liu et al. / Data in Brief 5 (2015) 1035–10471040
Table 1 (continued )
Y. Liu et al. / Data in Brief 5 (2015) 1035–1047 1041
Table 1 (continued )
Y. Liu et al. / Data in Brief 5 (2015) 1035–10471042
Table 1 (continued )
Y. Liu et al. / Data in Brief 5 (2015) 1035–1047 1043
Table 1 (continued )
Y. Liu et al. / Data in Brief 5 (2015) 1035–10471044
Table 1 (continued )
Y. Liu et al. / Data in Brief 5 (2015) 1035–1047 1045
Table 1 (continued )
Y. Liu et al. / Data in Brief 5 (2015) 1035–10471046coupled to AKTA Puriﬁer (GE Healthcare, Bio-Science Inc. Germany), previously equilibrated with
phosphate-buffered saline (PBS) containing 0.5 M NaCl. After washing with equilibrating buffer, the
adsorbed material was eluted with 0.1 M D-mannose in equilibrating buffer. The preparations
obtained were ultradiaﬁltered against PBS using a YM10 membrane (Amicon Division, W.R. Grace,
Beverly, MA) and biotinylated using sulfo-NHS-LC-biotin (Sigma-Aldrich, St. Louis, USA) according to
the manufacturer instructions.2.2. Glycan microarray analyses
Microarray analyses were performed using the neoglycolipid (NGL)-based system [4], with lipid-
linked glycan probes, including NGLs and glycolipids, and comprising a total of 255 oligosaccharides
(in-house designation ‘Array Sets 18–22bis’; list of probes are in Table 1). These were robotically
printed on nitrocellulose-coated glass slides, at 2 and 7 fmol per spot, using a non-contact arrayer
(Piezorray; PerkinElmer LAS, Beaconsﬁeld, UK). The microarray binding assays were performed as
described [1]. In brief, microarray slides were blocked at ambient temperature with 1% w/v bovine
serum albumin (BSA; Sigma-Aldrich) in casein blocker solution (Pierce Chemical Co, USA) for 1 h. The
biotinylated lectin samples were overlaid at 50 μg/mL, and binding was detected using Alexa Fluor
Y. Liu et al. / Data in Brief 5 (2015) 1035–1047 1047647-labeled streptavidin (Molecular Probes-Life Technologies, CA, USA) at 1 μg/mL in blocker solu-
tion. Glycoarray data analysis was performed with dedicated software [5]. The binding signals were
probe-dose dependent. The results of glycan probes at 7 fmol per spot are shown in Fig. 1 and Table 1.Funding sources
This study was supported by Grants from the Fundação de Amparo a Pesquisa do Estado de São
Paulo (2009/16146-9; 2006/60642-3, and 2013/04088-0), Conselho Nacional de Desenvolvimento
Cientíﬁco e Tecnológico (306503/2009-3; 306298/2013-9), Financiadora de Estudos e Projetos
(0110045900), by the United Kingdom Research Council Basic Technology Initiative Glycoarrays
and Translational Grants GRS/79268 and EP/G037604/1, and by Wellcome Trust Grants WT093378MA
and WT099197MA (to T F).Acknowledgments
We thank Dr. Maria Helena de Souza Goldman for providing the pYES-DEST52 expression vector
containing the ArtinM coding sequence. We also thank Dr. Sandro Gomes Soares and Dr. Ebert Seixas
Hanna from Invent Biotechnologies, for their help with y-ArtinM production and puriﬁcation. Sup-
ported by by the United Kingdom Research Councils Basic Technology Initiative Glycoarrays Grant
GRS/79268 and Translational Grant EP/G037604/1, and by Wellcome Trust Grants WT093378MA and
WT099197MA (to T. F.). The microarrays contain many glycans provided by collaborators whom we
thank as well as members of the Glycosciences Laboratory for their collaboration in the establishment
of the NGL-based microarray system.References
[1] N.T. Cecílio, F.C. Carvalho, Y. Liu, M. Moncrieffe, P.A.A. Buranello, A.L. Zorzetto-Fernandes, et al., Yeast expressed ArtinM
shares structure, carbohydrate recognition, and biological effects with native ArtinM, Int. J. Biol. Macromol. (2015), in press.
[2] M.A. Souza, F.C. Carvalho, L.P. Ruas, R. Ricci-Azevedo, M.C. Roque-Barreira, The immunomodulatory effect of plant lectins: a
review with emphasis on ArtinM properties, Glycoconj. J. 30 (2013) 641–657.
[3] V.S. Mariano, A.L. Zorzetto-Fernandes, T.A. da Silva, L.P. Ruas, L.L. Nohara, I.C. Almeida, M.C. Roque-Barreira, Recognition of
TLR2 N-glycans: critical role in ArtinM immunomodulatory activity, PLoS One 9 (6) (2014) e98512.
[4] Y. Liu, R.A. Childs, A.S. Palma, M.A. Campanero-Rhodes, M.S. Stoll, W. Chai, T. Feizi, Neoglycolipid-Based Oligosaccharide
Microarray System: preparation of NGLs and their noncovalent immobilization on nitrocellulose-coated glass slides for
microarray analyses, Methods Mol. Biol. 808 (2012) 117–136.
[5] M.S. Stoll, T. Feizi, Software tools for storing, processing and displaying carbohydrate microarray data, in: C. Kettner
(Ed.), Proceedings of the Beilstein Symposium on Glyco-Bioinformatics, 4–8 October, Potsdam, Germany, Beilstein Institute
for the Advancement of Chemical Sciences, Frankfurt, Germany, pp. 123–140, Available at 〈http://www.belisteininstitut.de/
download/613/09_stoll.pdf〉, 2009 (accessed 25.08.15).
[6] R. Santos-de-Oliveira, M. Dias-Barufﬁ, S.M. Thomaz, L.M. Beltramini, M.C. Roque-Barreira, A neutrophil migration-inducing
lectin from Artocarpus integrifolia, J. Immunol. 153 (4) (1994) 1798–1807.


Glycan microarray analysis of the carbohydrate-recognition specificity of native and recombinant forms of the lectin ArtinM 

Spiral - Imperial College Digital Repository

Contents lists available at ScienceDirectData in BriefData in Brief 5 (2015) 1035–1047http://d2352-34(http://cDOIn CorrE-mjournal homepage: www.elsevier.com/locate/dibData ArticleGlycan microarray analysis of thecarbohydrate-recognition specificity of nativeand recombinant forms of the lectin ArtinMY. Liu a,n, N.T. Cecílio b, F.C. Carvalho b, M.C. Roque-Barreira b,n,T. Feizi aa Glycosciences Laboratory, Department of Medicine, Imperial College London, London, United Kingdomb Departamento de Biologia Celular e Molecular e Bioagentes Patogênicos, Faculdade de Medicina de RibeirãoPreto, Universidade de São Paulo, Brazila r t i c l e i n f oArticle history:Received 8 October 2015Received in revised form6 November 2015Accepted 8 November 2015Available online 18 November 2015Keywords:Glycan microarrayLectinArtinMArtocarpus heterophyllusImmunomodulationx.doi.org/10.1016/j.dib.2015.11.01409/& 2015 The Authors. Published by Elsereativecommons.org/licenses/by-nc-nd/4.0of original article: http://dx.doi.org/10.1016esponding authors.ail addresses: yan.liu2@imperial.ac.uk (Y. Lia b s t r a c tThis article contains data related to the researc.h article entitled“Yeast-derived ArtinM shares structure, carbohydrate recognition,and biological effects with native ArtinM” by Cecílio et al. (2015)[1]. ArtinM, a D-mannose-binding lectin isolated from the seeds ofArtocarpus heterophyllus, exerts immunomodulatory and regen-erative activities through its Carbohydrate Recognition Domain(CRD) (Souza et al., 2013; Mariano et al., 2014 [2,3]). The limitedavailability of the native lectin (n-ArtinM) led us to characterize arecombinant form of the protein, obtained by expression in Sac-charomyces cerevisiae (y-ArtinM). We compared the carbohydrate-binding specificities of y-ArtinM and n-ArtinM by analyzing thebinding of biotinylated preparations of the two lectin forms using aneoglycolipid (NGL)-based glycan microarray. Data showed thaty-ArtinM mirrored the specificity exhibited by n-ArtinM.& 2015 The Authors. Published by Elsevier Inc. This is an openaccess article under the CC BY-NC-ND license(http://creativecommons.org/licenses/by-nc-nd/4.0/).vier Inc. This is an open access article under the CC BY-NC-ND license/)./j.ijbiomac.2015.09.062u), mcrbarre@fmrp.usp.br (M.C. Roque-Barreira).Y. Liu et al. / Data in Brief 5 (2015) 1035–10471036Specification TableSMTHDEEDDubject area Biologyore specific sub-ject areaGlycobiologyype of data Graphs and tableow data wasacquiredThe data were generated from a NGL-based microarray system [4]. Afterbinding analyses, the slide was scanned using ProScanArray microarrayscanner (PerkinElmer) and the image files were quantified using ScanArrayExpress software (PerkinElmer).ata format A dedicated in-house-designed software suite was used for storing, retriev-ing and displaying carbohydrate microarray data [5], here as histogramcharts (Fig. 1) and result table (Table 1).xperimentalfactorsn-ArtinM and y-ArtinM forms were biotinylated and analyzed for bindingusing a NGL-based microarray (in-house designation ‘Array Sets 18–22bis’)containing 255 lipid-linked glycan probes (Table 1).xperimentalfeaturesGlycan microarray analyses of an immunomodulatory lectinata sourcelocationUniversity of Sao Paulo, Brazil and Imperial College London, UK.ata accessibility The data are supplied with this article and will be online available at the WebPortal of Glycosciences Laboratory, Imperial College London: https://glycosciences.med.ic.ac.uk/data.html.Value of the data The wide spectrum of glycans that constitute the glycan microarray makes this platform suitable tocompare the carbohydrate-binding specificities exhibited by native and recombinant lectins. The data derived from the NGL-based microarray analyses provide important information on thecarbohydrate binding specificities of y-ArtinM and n-ArtinM, and serve as the basis for furtherstudies on the fine specificities of the lectins using other microarray systems or complementarytechniques.1. DataIn this study, we analyzed the native form of ArtinM and its yeast-derived counterpart, in terms oftheir ability to bind to 255 glycans distributed in a microarray platform, in order to identify whethern-ArtinM and y-ArtinM shared sugar-recognition specificity. Measurement of fluorescence intensityindicated that both preparations bound to N-glycan-related sequences (Fig. 1A and B), with a pre-ference for probes having the core trimannoside Manα1-3(Manα1-6) Man. This binding intensity wasenhanced when the probe contained a Fucose residue at the trimannoside core (Table 1 – probe 131);whereas binding was diminished when a similar position in the glycan was occupied by β1-2-linkedxylose (probes 130 and 132). Some differences between the two lectin forms were identified in themagnitude of binding to probes 129, 131, 133, 135, 147, 148, 149, 150, 152, 153, 158, 159 and 160. Ingeneral, y-ArtinM showed higher fluorescence intensity than n-ArtinM.Fig. 1. Carbohydrate microarray analyses of n-ArtinM (A) and y-ArtinM (B). Numerical scores of the binding signals are meansof duplicate spots at 7 fmol/spot (with error bars). The complete list of probes and their sequences and binding scores are inTable 1.Y. Liu et al. / Data in Brief 5 (2015) 1035–1047 10372. Materials and methods and data2.1. Sample preparationn-ArtinM was obtained from a saline extract of Artocarpus heterophyllus (jackfruit) seeds [6].Saccharomyces cerevisiae BJ3501 was used to express y-ArtinM and the lectin was obtained by yeastlysis [1]. n-ArtinM and y-ArtinM were purified by affinity chromatography on a D-mannose columnTable 1Oligosaccharide probes included in the microarray and the binding signals (means of the fluorescence intensity at 7 fmol/probespot) of n-ArtinM and y-ArtinM.Y. Liu et al. / Data in Brief 5 (2015) 1035–10471038Table 1 (continued )Y. Liu et al. / Data in Brief 5 (2015) 1035–1047 1039Table 1 (continued )Y. Liu et al. / Data in Brief 5 (2015) 1035–10471040Table 1 (continued )Y. Liu et al. / Data in Brief 5 (2015) 1035–1047 1041Table 1 (continued )Y. Liu et al. / Data in Brief 5 (2015) 1035–10471042Table 1 (continued )Y. Liu et al. / Data in Brief 5 (2015) 1035–1047 1043Table 1 (continued )Y. Liu et al. / Data in Brief 5 (2015) 1035–10471044Table 1 (continued )Y. Liu et al. / Data in Brief 5 (2015) 1035–1047 1045Table 1 (continued )Y. Liu et al. / Data in Brief 5 (2015) 1035–10471046coupled to AKTA Purifier (GE Healthcare, Bio-Science Inc. Germany), previously equilibrated withphosphate-buffered saline (PBS) containing 0.5 M NaCl. After washing with equilibrating buffer, theadsorbed material was eluted with 0.1 M D-mannose in equilibrating buffer. The preparationsobtained were ultradiafiltered against PBS using a YM10 membrane (Amicon Division, W.R. Grace,Beverly, MA) and biotinylated using sulfo-NHS-LC-biotin (Sigma-Aldrich, St. Louis, USA) according tothe manufacturer instructions.2.2. Glycan microarray analysesMicroarray analyses were performed using the neoglycolipid (NGL)-based system [4], with lipid-linked glycan probes, including NGLs and glycolipids, and comprising a total of 255 oligosaccharides(in-house designation ‘Array Sets 18–22bis’; list of probes are in Table 1). These were roboticallyprinted on nitrocellulose-coated glass slides, at 2 and 7 fmol per spot, using a non-contact arrayer(Piezorray; PerkinElmer LAS, Beaconsfield, UK). The microarray binding assays were performed asdescribed [1]. In brief, microarray slides were blocked at ambient temperature with 1% w/v bovineserum albumin (BSA; Sigma-Aldrich) in casein blocker solution (Pierce Chemical Co, USA) for 1 h. Thebiotinylated lectin samples were overlaid at 50 μg/mL, and binding was detected using Alexa FluorY. Liu et al. / Data in Brief 5 (2015) 1035–1047 1047647-labeled streptavidin (Molecular Probes-Life Technologies, CA, USA) at 1 μg/mL in blocker solu-tion. Glycoarray data analysis was performed with dedicated software [5]. The binding signals wereprobe-dose dependent. The results of glycan probes at 7 fmol per spot are shown in Fig. 1 and Table 1.Funding sourcesThis study was supported by Grants from the Fundação de Amparo a Pesquisa do Estado de SãoPaulo (2009/16146-9; 2006/60642-3, and 2013/04088-0), Conselho Nacional de DesenvolvimentoCientífico e Tecnológico (306503/2009-3; 306298/2013-9), Financiadora de Estudos e Projetos(0110045900), by the United Kingdom Research Council Basic Technology Initiative Glycoarraysand Translational Grants GRS/79268 and EP/G037604/1, and by Wellcome Trust Grants WT093378MAand WT099197MA (to T F).AcknowledgmentsWe thank Dr. Maria Helena de Souza Goldman for providing the pYES-DEST52 expression vectorcontaining the ArtinM coding sequence. We also thank Dr. Sandro Gomes Soares and Dr. Ebert SeixasHanna from Invent Biotechnologies, for their help with y-ArtinM production and purification. Sup-ported by by the United Kingdom Research Councils Basic Technology Initiative Glycoarrays GrantGRS/79268 and Translational Grant EP/G037604/1, and by Wellcome Trust Grants WT093378MA andWT099197MA (to T. F.). The microarrays contain many glycans provided by collaborators whom wethank as well as members of the Glycosciences Laboratory for their collaboration in the establishmentof the NGL-based microarray system.References[1] N.T. Cecílio, F.C. Carvalho, Y. Liu, M. Moncrieffe, P.A.A. Buranello, A.L. Zorzetto-Fernandes, et al., Yeast expressed ArtinMshares structure, carbohydrate recognition, and biological effects with native ArtinM, Int. J. Biol. Macromol. (2015), in press.[2] M.A. Souza, F.C. Carvalho, L.P. Ruas, R. Ricci-Azevedo, M.C. Roque-Barreira, The immunomodulatory effect of plant lectins: areview with emphasis on ArtinM properties, Glycoconj. J. 30 (2013) 641–657.[3] V.S. Mariano, A.L. Zorzetto-Fernandes, T.A. da Silva, L.P. Ruas, L.L. Nohara, I.C. Almeida, M.C. Roque-Barreira, Recognition ofTLR2 N-glycans: critical role in ArtinM immunomodulatory activity, PLoS One 9 (6) (2014) e98512.[4] Y. Liu, R.A. Childs, A.S. Palma, M.A. Campanero-Rhodes, M.S. Stoll, W. Chai, T. Feizi, Neoglycolipid-Based OligosaccharideMicroarray System: preparation of NGLs and their noncovalent immobilization on nitrocellulose-coated glass slides formicroarray analyses, Methods Mol. Biol. 808 (2012) 117–136.[5] M.S. Stoll, T. Feizi, Software tools for storing, processing and displaying carbohydrate microarray data, in: C. Kettner(Ed.), Proceedings of the Beilstein Symposium on Glyco-Bioinformatics, 4–8 October, Potsdam, Germany, Beilstein Institutefor the Advancement of Chemical Sciences, Frankfurt, Germany, pp. 123–140, Available at 〈http://www.belisteininstitut.de/download/613/09_stoll.pdf〉, 2009 (accessed 25.08.15).[6] R. Santos-de-Oliveira, M. Dias-Baruffi, S.M. Thomaz, L.M. Beltramini, M.C. Roque-Barreira, A neutrophil migration-inducinglectin from Artocarpus integrifolia, J. Immunol. 153 (4) (1994) 1798–1807.

Glycan microarray analysis of the carbohydrate-recognition specificity of native and recombinant forms of the lectin ArtinM

This article contains data related to the researc.h article entitled “Yeast-derived ArtinM shares structure, carbohydrate recognition, and biological effects with native ArtinM” by Cecílio et al. (2015) [1]. ArtinM, a D-mannose-binding lectin isolated from the seeds of Artocarpus heterophyllus, exerts immunomodulatory and regenerative activities through its Carbohydrate Recognition Domain (CRD) (Souza et al., 2013; Mariano et al., 2014 [2,3]). The limited availability of the native lectin (n-ArtinM) led us to characterize a recombinant form of the protein, obtained by expression in Saccharomyces cerevisiae (y-ArtinM). We compared the carbohydrate-binding specificities of y-ArtinM and n-ArtinM by analyzing the binding of biotinylated preparations of the two lectin forms using a neoglycolipid (NGL)-based glycan microarray. Data showed that y-ArtinM mirrored the specificity exhibited by n-ArtinM

Y. Liu

N.T. Cecílio

F.C. Carvalho

M.C. Roque-Barreira

T. Feizi

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Glycan microarray analysis of the carbohydrate-recognition specificity of native and recombinant forms of the lectin ArtinM

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