liu.seSearch for publications in DiVA
Change search
Link to record
Permanent link

Direct link
BETA
Rodriguez, Jesus
Alternative names
Publications (4 of 4) Show all publications
Rydell, G. E., Nilsson, J., Rodriguez, J., Ruvoen-Clouet, N., Svensson, L., Le Pendu, J. & Larson , G. (2009). Human noroviruses recognize sialyl Lewis x neoglycoprotein. Glycobiology, 19(3), 309-320
Open this publication in new window or tab >>Human noroviruses recognize sialyl Lewis x neoglycoprotein
Show others...
2009 (English)In: Glycobiology, ISSN 0959-6658, E-ISSN 1460-2423, Vol. 19, no 3, p. 309-320Article in journal (Refereed) Published
Abstract [en]

The carbohydrate binding characteristics of a norovirus GII.3 (Chron1) and a GII.4 (Dijon) strain were investigated using virus-like particles (VLPs) and saliva samples from 81 individuals genotyped for FUT2 (secretor) and FUT3 (Lewis) and phenotyped for ABO and Lewis blood groups. The two VLPs showed a typical secretor-gene-dependent binding and bound significantly stronger to saliva from A, B, and AB than from O individuals (P < 0.0001 and P < 0.001) but did not bind to any samples from secretor-negative individuals. The GII.3 strain showed larger interindividual variation and bound stronger to saliva from B than from A(2) secretors (P < 0.01). When assaying for binding to neoglycoproteins, the GII.3 and GII.4 strains were compared with the Norwalk GI.1 prototype strain. Although all three strains bound to Lewis b (and H type 1 chain) glycoconjugates, only the two GII strains showed an additional binding to sialyl Lewis x. This novel binding was specific since the VLPs did not bind to structural analogs, e.g., Lewis x or sialyl Lewis a, but only to sialyl Lewis x, sialyl diLewis x and sialylated type 2 chain conjugates. In inhibition experiments, the sialyl Lewis x conjugate was the most potent inhibitor. The minimal requirement for this potential receptor structure is Neu5Ac alpha 3Gal beta 4(Fuc alpha 3)GlcNAc beta 3Gal beta- where Fuc is not absolutely necessary for binding. Our study shows that some human norovirus GII strains have at least two binding specificities: one secretor-gene-dependent related to alpha 1,2-fucosylated carbohydrates and another related to alpha 2,3-sialylated carbohydrates of the type 2 chain, e.g., sialyl Lewis x.

Keywords
norovirus, neoglycoprotein, secretor, sialyl Lewis x, virus-like particle
National Category
Medical and Health Sciences
Identifiers
urn:nbn:se:liu:diva-16733 (URN)10.1093/glycob/cwn139 (DOI)
Available from: 2009-02-14 Created: 2009-02-13 Last updated: 2017-12-14
Karlsson, B., Michael Lindberg, A., Rodriguez-Diaz, J., Hedlund, K.-O., Persson, B. & Svensson , L. (2009). Quasispecies dynamics and molecular evolution of human norovirus capsid P region during chronic infection. Journal of General Virology, 90, 432-441
Open this publication in new window or tab >>Quasispecies dynamics and molecular evolution of human norovirus capsid P region during chronic infection
Show others...
2009 (English)In: Journal of General Virology, ISSN 0022-1317, E-ISSN 1465-2099, Vol. 90, p. 432-441Article in journal (Refereed) Published
Abstract [en]

In this novel study, we have for the first time identified evolutionarily conserved capsid residues in an individual chronically infected with norovirus (GGII.3). From 2000 to 2003, a total of 147 P1-1 and P2 capsid sequences were sequenced and investigated for evolutionarily conserved and functionally important residues by the evolutionary trace (ET) algorithm. The ET algorithm revealed more absolutely conserved residues (ACR) in the P1-1 domain (47/53, 88 %) as compared with the P2 domain (86/133, 64 %). The capsid P1-1 and P2 domains evolved in time-dependent manner, with a distinct break point observed between autumn/winter of year 2000 (isolates P1, P3 and P5) and spring to autumn of year 2001 (isolates P11, P13 and P15), which presumably coincided with a change of clinical symptoms. Furthermore, the ET analysis revealed a similar receptor-binding pattern as reported for Norwalk and VA387 strains, with the CS-4 and CS-5 patch (Norwalk strain) including residues 329 and 377 and residues 306 and 310, respectively, all being ACR in all partitions. Most interesting was that residues 343, 344, 345, 374, 390 and 391 of the proposed receptor A and B trisaccharide binding site (VA387 strain) within the P2 domain remained ACR in all partitions, presumably because there was no selective advantage to alter the histo blood group antigens (HBGA) receptor binding specificity. In conclusion, this study provides novel insights to the evolutionary process of norovirus during chronic infection.

National Category
Medical and Health Sciences
Identifiers
urn:nbn:se:liu:diva-16852 (URN)10.1099/vir.0.005082-0 (DOI)
Available from: 2009-02-21 Created: 2009-02-20 Last updated: 2017-12-13
Rodriguez, J., Rubilar-Abreu, E., Spitzner, M., Hedlund, K.-O., Liprandi, F. & Svensson, L. (2008). Design of a multiplex nested PCR for genotyping of the NSP4 from group A rotavirus. Journal of Virological Methods, 149(2), 240-245
Open this publication in new window or tab >>Design of a multiplex nested PCR for genotyping of the NSP4 from group A rotavirus
Show others...
2008 (English)In: Journal of Virological Methods, ISSN 0166-0934, E-ISSN 1879-0984, Vol. 149, no 2, p. 240-245Article in journal (Refereed) Published
Abstract [en]

A novel PCR method was developed to discriminate amongst genotypes A-C of the rotavirus non-structural protein 4 (NSP4). Genotype-specific primers were designed that correctly identified the NSP4 genotype when evaluated as a multiplex PCR with cell culture adapted rotavirus strains. Rotavirus strains B223 SGIG6P6[1], NCDV SGIG6P6[1] and SA11 SGIG3P5B[2] were used as control for NSP4 genotype A, A34 SGIG5P14[23], Gottfried SGIIG4P2B[6] and Wa SGIIG1P1A[8] for NSP4 genotype B, RRV SGIG3P5B[3] for NSP4 genotype C. Subsequently, the same set of specific primers was used to genotype a set of 77 Swedish clinical samples. The results showed that all human clinical samples analyzed belong to the NSP4 genotype B and the VP6 subgroup II. © 2008 Elsevier B.V. All rights reserved.

National Category
Medical and Health Sciences
Identifiers
urn:nbn:se:liu:diva-43457 (URN)10.1016/j.jviromet.2008.01.030 (DOI)73896 (Local ID)73896 (Archive number)73896 (OAI)
Available from: 2009-10-10 Created: 2009-10-10 Last updated: 2017-12-13
Rydell, G. E., Nilsson, J., Rodriguez, J., Ruvoen-Clouet, N., Svensson, L., le Pendu, J. & Larson , G. (2008). Human Noroviruses Recognize Sialyl Lewis x Neoglycoprotein. In: 2008 Meeting of the Society for Glycobiology: (pp. 1000-1001). , 18(11)
Open this publication in new window or tab >>Human Noroviruses Recognize Sialyl Lewis x Neoglycoprotein
Show others...
2008 (English)In: 2008 Meeting of the Society for Glycobiology, 2008, Vol. 18, no 11, p. 1000-1001Conference paper, Published paper (Refereed)
National Category
Medical and Health Sciences
Identifiers
urn:nbn:se:liu:diva-16354 (URN)10.1093/glycob/cwn086 (DOI)
Available from: 2009-01-16 Created: 2009-01-16 Last updated: 2009-01-16
Organisations

Search in DiVA

Show all publications