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dc.contributor.author
Martinez, María Guadalupe  
dc.contributor.author
Prado Acosta, Mariano  
dc.contributor.author
Candurra, Nélida Alicia  
dc.contributor.author
Ruzal, Sandra Mónica  
dc.date.available
2025-09-05T11:34:14Z  
dc.date.issued
2012-06  
dc.identifier.citation
Martinez, María Guadalupe; Prado Acosta, Mariano; Candurra, Nélida Alicia; Ruzal, Sandra Mónica; S-layer proteins of Lactobacillus acidophilus inhibits JUNV infection; Academic Press Inc Elsevier Science; Biochemical and Biophysical Research Communications; 422; 4; 6-2012; 590-595  
dc.identifier.issn
0006-291X  
dc.identifier.uri
http://hdl.handle.net/11336/270398  
dc.description.abstract
It has been previously described that S-layer binds to the C-type lectin DC-specific ICAM-3-grabbing nonintegrin (DC-SIGN, CD209). It was also shown that DC-SIGN is a cell-surface adhesion factor that enhances viral entry of several virus families. Among those, Junin virus (JUNV) entry is enhanced in cells expressing DC-SIGN and for that reason surface-layer protein (S-layer) of Lactobacillus acidophilus ATCC 4365 was evaluated as a possible JUNV inhibitor. Experiments using 3T3 cells stably expressing DC- SIGN, showed an almost complete inhibition of JUNV infection when they were treated with S-layer in a similar extend as the inhibition shown by mannan. However no inhibition effect was observed in 3T3 wild type cells or in 3T3 cells expressing liver/lymph node-specific ICAM-3 grabbing nonintegrin (L-SIGN or DC-SIGNR or CD209L). Treatments with S-layer during different times in the infection demonstrated that inhibition was only observed when S-layer was presented in early stages of the viral infection. This inhibition does not involve the classic recognition of mannose by this C-type lectin as the S-layer showed no evidence to be glycosylated. In fact, the highly basic nature of the S-layer (pI>9.5) seems to be involved in electrostatic interactions between DC-SIGN and S-layer, since high pH abolished the inhibitory effect on infection cause by the S-layer. In silico analysis predicts a Ca2+dependant carbohydrate recognition domain in the SlpA protein. This novel characteristic of the S-layer, a GRAS status protein, contribute to the pathogen exclusion reported for this probiotic strain and may be applied as an antiviral agent to inhibit several kinds of viruses.  
dc.format
application/pdf  
dc.language.iso
eng  
dc.publisher
Academic Press Inc Elsevier Science  
dc.rights
info:eu-repo/semantics/openAccess  
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/  
dc.subject
Surface Layer  
dc.subject
Lactobacillus  
dc.subject
antiviral  
dc.subject.classification
Biología Celular, Microbiología  
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Ciencias Biológicas  
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CIENCIAS NATURALES Y EXACTAS  
dc.title
S-layer proteins of Lactobacillus acidophilus inhibits JUNV infection  
dc.type
info:eu-repo/semantics/article  
dc.type
info:ar-repo/semantics/artículo  
dc.type
info:eu-repo/semantics/publishedVersion  
dc.date.updated
2025-09-04T12:11:02Z  
dc.journal.volume
422  
dc.journal.number
4  
dc.journal.pagination
590-595  
dc.journal.pais
Países Bajos  
dc.journal.ciudad
Amsterdam  
dc.description.fil
Fil: Martinez, María Guadalupe. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina  
dc.description.fil
Fil: Prado Acosta, Mariano. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina  
dc.description.fil
Fil: Candurra, Nélida Alicia. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina  
dc.description.fil
Fil: Ruzal, Sandra Mónica. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina  
dc.journal.title
Biochemical and Biophysical Research Communications  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0006291X12008959?v=s5  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.bbrc.2012.05.031