Silvia Sandini

Dr. Silvia Sandini

orcid

Research Focus & Metrics

Academic Career Length

30Years (1997-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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1 June 2012 in Vaccine
Verified
Journal Article
Closed access
FBFlavia De Bernardis
Flavia De Bernardis
MAMario Amacker
Mario Amacker
SASilvia Arancia
Silvia Arancia
SSSilvia Sandini
Silvia Sandini
CGChristel Gremion
Christel Gremion
ACAntonio Cassone
Antonio Cassone

1 January 2007 in The Journal of Infectious Diseases
Verified
Journal Article
Open access
PDF file
FBFlavia De Bernardis
Flavia De Bernardis
HLHaiqun Liu
Haiqun Liu
RORachel O’mAhony
Rachel O’mAhony
RVRoberto La Valle
Roberto La Valle
SBSilvia Bartollino
Silvia Bartollino
ACAntonio Cassone
Antonio Cassone
Antibody variable domains (domain antibodies [DAbs]) are genetically engineered antibody fragments that include individual heavy-chain (VH) or κ-chai

1 July 2011 in FEMS Immunology & Medical Microbiology
Verified
Journal Article
Open access
PDF file
SSSilvia Sandini
Silvia Sandini
RVRoberto La Valle
Roberto La Valle
SDSilvia Deaglio
Silvia Deaglio
Fabio MalavasiFabio Malavasi
Fabio Malavasi
ACAntonio Cassone
Antonio Cassone
FBFlavia De Bernardis
Flavia De Bernardis
Sap2 (secreted aspartyl proteinase2) is a member of the Sap family of Candida albicans, a human opportunistic pathogen, which acts as a virulence fac

1 May 2007 in Cellular Microbiology
Verified
Journal Article
Closed access
PDF file
SSSilvia Sandini
Silvia Sandini
RVRoberto La Valle
Roberto La Valle
FBFlavia De Bernardis
Flavia De Bernardis
CMCaterina Macrì
Caterina Macrì
ACAntonio CassoneV
Antonio CassoneV
Mannoproteins are fungal cell wall components which play a main role in host-parasite relationship. Camp65p is a putative beta-glucanase mannoprotein of 65 kDa which has been characterized as a main target of human immune response against Candida albicans. However, nothing is known about its specific contribution to the biology and virulence of this fungus. We constructed CAMP65 knock-out mutants including null camp65/camp65 and CAMP65/camp65 heterozygous strains. The null strains had the same growth rate and morphology under yeast form as the wild-type strain but they were severely affected in hyphal morphogenesis both in vitro and in vivo. Hyphae formation was restored in revertant strains. The null mutants lost adherence to the plastic, and this was in keeping with the strong inhibition of fungal cell adherence to plastic exerted by anti-Camp65p antibodies. The null mutants were also significantly less virulent than the parental strains, and this loss of virulence was observed both in systemic and in mucosal C. albicans infection models. Nonetheless, the virulence in both infectious models was regained by the CAMP65 revertants. Thus, CAMP65 of C. albicans encodes a putative beta-glucanase, mannoprotein adhesin, which has a dual role (hyphal cell wall construction and virulence), accounting for the particular relevance of host immune response against this mannoprotein.

1 March 2013 in International Journal of Medical Microbiology
Verified
Journal Article
Closed access
ABAlessia Bertini
Alessia Bertini
FBFlavia De Bernardis
Flavia De Bernardis
LHLambert A.M. Hensgens
Lambert A.M. Hensgens
SSSilvia Sandini
Silvia Sandini
SSSonia Senesi
Sonia Senesi
Arianna TavantiArianna Tavanti
Arianna Tavanti

1 January 2011 in BMC Microbiology
Verified
Journal Article
Open access
PDF file
SSSilvia Sandini
Silvia Sandini
Annarita StringaroAnnarita Stringaro
Annarita Stringaro
SASilvia Arancia
Silvia Arancia
Marisa ColoneMarisa Colone
Marisa Colone
Francesca MondelloFrancesca Mondello
Francesca Mondello
FBFlavia De Bernardis
Flavia De Bernardis
The MP65 gene of Candida albicans (orf19.1779) encodes a putative β-glucanase mannoprotein of 65 kDa, which plays a main role in a host-fungus relationship, morphogenesis and pathogenicity. In this study, we performed an extensive analysis of a mp65Δ mutant to assess the role of this protein in cell wall integrity, adherence to epithelial cells and biofilm formation.