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Université de Fribourg

The yeast cell wall protein Pry3 inhibits mating through highly conserved residues within the CAP domain

Cottier, Stéphanie ; Darwiche, Rabih ; Meyenhofer, Felix ; Debelyy, Mykhaylo O. ; Schneiter, Roger

In: Biology Open, 2020, vol. 9, no. 6, p. bio053470

Members of the CAP/SCP/TAPS superfamily have been implicated in many different physiological processes, including pathogen defense, sperm maturation and fertilization. The mode of action of this class of proteins, however, remains poorly understood. The genome of Saccharomyces cerevisiae encodes three CAP superfamily members, Pry1-3. We have previously shown that Pry1 function is required...

Università della Svizzera italiana

Virus-like particles and nanoparticles for vaccine development against HCMV

Perotti, Michela ; Perez, Laurent

In: Viruses, 2020, vol. 12, no. 1, p. 17 p

Human cytomegalovirus (HCMV) infects more than 70% of the human population worldwide. HCMV is responsible for high morbidity and mortality in immunocompromised patients and remains the leading viral cause of congenital birth defects. Despite considerable efforts in vaccine and therapeutic development, HCMV infection still represents an unmet clinical need and a life-threatening disease in...

Università della Svizzera italiana

Phenotype and specificity of T cells in primary human cytomegalovirus infection during pregnancy : IL-7Rpos long-term memory phenotype is associated with protection from vertical transmission

Mele, Federico ; Fornara, Chiara ; Jarrossay, David ; Furione, Milena ; Arossa, Alessia ; Spinillo, Arsenio ; Lanzavecchia, Antonio ; Gerna, Giuseppe ; Sallusto, Federica ; Lilleri, Daniele

In: Plos one, 2017, vol. 12, no. 11, p. e0187731

Congenital human cytomegalovirus (HCMV) infection is the major cause of birth defects and a precise definition of the HCMV-specific T-cell response in primary infection may help define reliable correlates of immune protection during pregnancy. In this study, a high throughput method was used to define the frequency of CD4+ and CD8+ T cells specific for four HCMV proteins in the naïve...

Università della Svizzera italiana

HCMV envelope glycoprotein diversity demystified

Foglierini, Mathilde ; Marcandalli, Jessica ; Perez, Laurent

In: Frontiers in microbiology, 2019, vol. 10, p. 1005

Human cytomegalovirus (HCMV) is the leading viral cause of congenital birth defects and is responsible for morbidity and mortality in immunosuppressed individuals. Considerable efforts have been deployed over the last decade to develop a vaccine capable of preventing HCMV infection. However, in recent clinical trials, vaccines showed at best modest efficacy in preventing infection. These...

Università della Svizzera italiana

Fetal human cytomegalovirus transmission correlates with delayed maternal antibodies to gH/gL/pUL128-130-131 complex during primary infection

Lilleri, Daniele ; Kabanova, Anna ; Revello, Maria Grazia ; Percivalle, Elena ; Sarasini, Antonella ; Genini, Emilia ; Sallusto, Federica ; Lanzavecchia, Antonio ; Corti, Davide ; Gerna, Giuseppe

In: Plos one, 2013, vol. 8, no. 3, p. e59863

Primary human cytomegalovirus (HCMV) infections during pregnancy are associated with a high risk of virus transmission to the fetus. To identify correlates of intrauterine HCMV transmission, serial serum samples from HCMV transmitter and non-transmitter pregnant women with primary HCMV infection were analyzed for the presence of neutralizing antibodies against different glycoproteins and...

Università della Svizzera italiana

The human transmembrane protease serine 2 is necessary for the production of group 2 influenza A virus pseudotypes

Ferrara, Francesca ; Molesti, Eleonora ; Böttcher-Friebertshäuser, Eva ; Cattoli, Giovanni ; Corti, Davide ; Scott, Simon D. ; Temperton, Nigel J.

In: Journal of molecular and genetic medicine, 2013, vol. 7, p. 309-314

The monomer of influenza haemagglutinin is synthesized as a single polypeptide precursor that during maturation is cleaved by proteases into two active subunits. Other studies have demonstrated that the human Transmembrane Protease Serine 2 (TMPRSS2) can cleave the HA of human seasonal influenza viruses. Consequently, we have investigated the use of human Transmembrane Protease Serine 2 to...

Università della Svizzera italiana

Antibody-driven design of a human cytomegalovirus gHgLpUL128L subunit vaccine that selectively elicits potent neutralizing antibodies

Kabanovaa, Anna ; Perez, Laurent ; Lilleri, Daniele ; Marcandalli, Jessica ; Agatic, Gloria ; Becattini, Simone ; Preite, Silvia ; Fuschillo, Dario ; Percivalle,Elena ; Sallusto, Federica ; Gerna, Giuseppe ; Corti, Davide ; Lanzavecchia, Antonio

In: Proceedings of the national academy of sciences of the United States of America, 2014, vol. 111, no. 50, p. 17965-17970

The use of neutralizing antibodies to identify the most effective antigen has been proposed as a strategy to design vaccines capable of eliciting protective B-cell immunity. In this study, we analyzed the human antibody response to cytomegalovirus (human cytomegalovirus, HCMV) infection and found that antibodies to glycoprotein (g)B, a surface glycoprotein that has been developed as a HCMV...

Università della Svizzera italiana

Isolation of human monoclonal antibodies that potently neutralize human cytomegalovirus infection by targeting different epitopes on the gH/gL/UL128-131A complex

Macagno, Annalisa ; Bernasconi, Nadia L. ; Vanzetta, Fabrizia ; Dander, Erica ; Sarasini, Antonella ; Revello, Maria Grazia ; Gerna, Giuseppe ; Sallusto, Federica ; Lanzavecchia, Antonio

In: Journal of Virology, 2010, vol. 84, no. 2, p. 1005-1013

Human cytomegalovirus (HCMV) is a widely circulating pathogen that causes severe disease in immunocompromised patients and infected fetuses. By immortalizing memory B cells from HCMV-immune donors, we isolated a panel of human monoclonal antibodies that neutralized at extremely low concentrations (90% inhibitory concentration [IC90] values ranging from 5 to 200 pM) HCMV infection of...

Consortium of Swiss Academic Libraries

Transmembrane segment proteases

Martoglio, B.

In: Protoplasma, 1999, vol. 207, no. 3-4, p. 141-146