This page has only limited features, please log in for full access.

Unclaimed
Gabriele Anichini
Virology Unit, Department of Medical Biotechnologies, University of Siena, 53100 Siena, Italy

Honors and Awards

The user has no records in this section


Career Timeline

The user has no records in this section.


Short Biography

Gabriele Anichini has developed immunological expertise by studying the humoral and cell-mediated response in subjects vaccinated against measles virus following the recent epidemic. Recently, he conducted similar studies on patients vaccinated against COVID-19.

Following
Followers
Co Authors
The list of users this user is following is empty.
Following: 0 users

Feed

Journal article
Published: 19 August 2021 in Vaccines
Reads 0
Downloads 0

Emerging and re-emerging viral infections have been an important public health problem in recent years. We focused our attention on Toscana virus (TOSV), an emergent neurotropic negative-strand RNA virus of the Phenuiviridae family. The mechanisms of protection against phlebovirus natural infection are not known; however, it is supposed that a virus-neutralizing antibody response against viral glycoproteins would be useful to block the first stages of infection. By using an improved memory B cell immortalization method, we obtained a panel of human mAbs which reacted with TOSV antigens. We identified three epitopes of TOSV Gn glycoproteins by neutralizing mAbs using synthetic peptide arrays on membrane support (SPOT synthesis). These epitopes, separated in primary structure, might be exposed near one another as a conformational epitope in their native structure. In vivo studies were conducted to evaluate the humoral response elicited in mice immunized with the identified peptides. The results underlined the hypothesis that the first two peptides located in the NH2 terminus could form a conformational epitope, while the third, located near the transmembrane sequence in the carboxyl terminus, was necessary to strengthen neutralizing activity. Our results emphasize the importance of identifying neutralizing epitopes shared among the various phleboviruses, which could be exploited for the development of a potential epitope-based diagnostic assay or a polyvalent protective vaccine against different phleboviruses.

ACS Style

Claudia Gandolfo; Shibily Prathyumn; Chiara Terrosi; Gabriele Anichini; Gianni Gori Savellini; Davide Corti; Luisa Bracci; Antonio Lanzavecchia; Gleyder Roman-Sosa; Maria Grazia Cusi. Identification of a Neutralizing Epitope on TOSV Gn Glycoprotein. Vaccines 2021, 9, 924 .

AMA Style

Claudia Gandolfo, Shibily Prathyumn, Chiara Terrosi, Gabriele Anichini, Gianni Gori Savellini, Davide Corti, Luisa Bracci, Antonio Lanzavecchia, Gleyder Roman-Sosa, Maria Grazia Cusi. Identification of a Neutralizing Epitope on TOSV Gn Glycoprotein. Vaccines. 2021; 9 (8):924.

Chicago/Turabian Style

Claudia Gandolfo; Shibily Prathyumn; Chiara Terrosi; Gabriele Anichini; Gianni Gori Savellini; Davide Corti; Luisa Bracci; Antonio Lanzavecchia; Gleyder Roman-Sosa; Maria Grazia Cusi. 2021. "Identification of a Neutralizing Epitope on TOSV Gn Glycoprotein." Vaccines 9, no. 8: 924.

Journal article
Published: 23 July 2021 in Viruses
Reads 0
Downloads 0

A weak production of INF-β along with an exacerbated release of pro-inflammatory cytokines have been reported during infection by the novel SARS-CoV-2 virus. SARS-CoV-2 encodes several proteins able to counteract the host immune system, which is believed to be one of the most important features contributing to the viral pathogenesis and development of a severe clinical picture. Previous reports have demonstrated that SARS-CoV-2 N protein, along with some non-structural and accessory proteins, efficiently suppresses INF-β production by interacting with RIG-I, an important pattern recognition receptor (PRR) involved in the recognition of pathogen-derived molecules. In the present study, we better characterized the mechanism by which the SARS-CoV-2 N counteracts INF-β secretion and affects RIG-I signaling pathways. In detail, when the N protein was ectopically expressed, we noted a marked decrease in TRIM25-mediated RIG-I activation. The capability of the N protein to bind to, and probably mask, TRIM25 could be the consequence of its antagonistic activity. Furthermore, this interaction occurred at the SPRY domain of TRIM25, harboring the RNA-binding activity necessary for TRIM25 self-activation. Here, we describe new findings regarding the interplay between SARS-CoV-2 and the IFN system, filling some gaps for a better understanding of the molecular mechanisms affecting the innate immune response in COVID-19.

ACS Style

Gianni Gori Savellini; Gabriele Anichini; Claudia Gandolfo; Maria Cusi. SARS-CoV-2 N Protein Targets TRIM25-Mediated RIG-I Activation to Suppress Innate Immunity. Viruses 2021, 13, 1439 .

AMA Style

Gianni Gori Savellini, Gabriele Anichini, Claudia Gandolfo, Maria Cusi. SARS-CoV-2 N Protein Targets TRIM25-Mediated RIG-I Activation to Suppress Innate Immunity. Viruses. 2021; 13 (8):1439.

Chicago/Turabian Style

Gianni Gori Savellini; Gabriele Anichini; Claudia Gandolfo; Maria Cusi. 2021. "SARS-CoV-2 N Protein Targets TRIM25-Mediated RIG-I Activation to Suppress Innate Immunity." Viruses 13, no. 8: 1439.

Brief report
Published: 18 May 2021 in Vaccines
Reads 0
Downloads 0

Due to their increased transmissibility, three variants of high concern have emerged in the United Kingdom (also known as B.1.1.7 lineage or VOC-202012/01), South Africa (B.1.351 lineage), and Brazil (P1 lineage) with multiple substitutions in the spike protein. Since neutralizing antibodies elicited by vaccination are likely considered as correlates of protection for SARS-CoV-2 infection, it is important to analyze whether vaccinees with mRNA BNT162b2 are equally protected against these emerging SARS-CoV-2 variants. To this aim, we enrolled healthy subjects one month after complete vaccination with Comirnaty and evaluated the neutralizing response against the native Wuhan strain and the emerging B.1.1.7, B.1.351 and P1 lineages, by using the microneutralization assay, currently considered the gold standard test for the evaluation and detection of functional neutralizing antibodies. The most remarkable finding of this study was the significantly lower neutralizing antibody titer against B.1.351 lineage, compared to the wild-type virus. No significant differences were observed with the other two lineages. These findings provide evidence that vaccinated subjects may not be equally protected against all SARS-CoV-2 lineages.

ACS Style

Gabriele Anichini; Chiara Terrosi; Gianni Gori Savellini; Claudia Gandolfo; Federico Franchi; Maria Cusi. Neutralizing Antibody Response of Vaccinees to SARS-CoV-2 Variants. Vaccines 2021, 9, 517 .

AMA Style

Gabriele Anichini, Chiara Terrosi, Gianni Gori Savellini, Claudia Gandolfo, Federico Franchi, Maria Cusi. Neutralizing Antibody Response of Vaccinees to SARS-CoV-2 Variants. Vaccines. 2021; 9 (5):517.

Chicago/Turabian Style

Gabriele Anichini; Chiara Terrosi; Gianni Gori Savellini; Claudia Gandolfo; Federico Franchi; Maria Cusi. 2021. "Neutralizing Antibody Response of Vaccinees to SARS-CoV-2 Variants." Vaccines 9, no. 5: 517.

Journal article
Published: 01 May 2021 in International Journal of Infectious Diseases
Reads 0
Downloads 0

We report the finding of SARS-CoV-2 genome in the corpse of an exhumed infected person, one month after her death. The viral gene targets were still present in her lungs and heart, however, the virus was no longer alive. Infectious risks from human corpses should be considered.

ACS Style

Mario Gabbrielli; Claudia Gandolfo; Gabriele Anichini; Tommaso Candelori; Matteo Benvenuti; Gianni Gori Savellini; Maria Grazia Cusi. How long can SARS-CoV-2 persist in human corpses? International Journal of Infectious Diseases 2021, 106, 1 -2.

AMA Style

Mario Gabbrielli, Claudia Gandolfo, Gabriele Anichini, Tommaso Candelori, Matteo Benvenuti, Gianni Gori Savellini, Maria Grazia Cusi. How long can SARS-CoV-2 persist in human corpses? International Journal of Infectious Diseases. 2021; 106 ():1-2.

Chicago/Turabian Style

Mario Gabbrielli; Claudia Gandolfo; Gabriele Anichini; Tommaso Candelori; Matteo Benvenuti; Gianni Gori Savellini; Maria Grazia Cusi. 2021. "How long can SARS-CoV-2 persist in human corpses?" International Journal of Infectious Diseases 106, no. : 1-2.

Journal article
Published: 12 October 2020 in Viruses
Reads 0
Downloads 0

The non-structural protein NSs of the Phenuiviridae family members appears to have a role in the host immunity escape. The stability of Toscana virus (TOSV) NSs protein was tested by a cycloheximide (CHX) chase approach on cells transfected with NSs deleted versions fused to a reporter gene. The presence of intrinsically disordered regions (IDRs) both at the C- and N-terminus appeared to affect the protein stability. Indeed, the NSsΔC and NSsΔN proteins were more stable than the wild-type NSs counterpart. Since TOSV NSs exerts its inhibitory function by triggering RIG-I for proteasomal degradation, the interaction of the ubiquitin system and TOSV NSs was further examined. Chase experiments with CHX and the proteasome inhibitor MG-132 demonstrated the involvement of the ubiquitin-proteasome system in controlling NSs protein amount expressed in the cells. The analysis of TOSV NSs by mass spectrometry allowed the direct identification of K104, K109, K154, K180, K244, K294, and K298 residues targeted for ubiquitination. Analysis of NSs K-mutants confirmed the presence and the important role of lysine residues located in the central and the C-terminal parts of the protein in controlling the NSs cellular level. Therefore, we directly demonstrated a new cellular pathway involved in controlling TOSV NSs fate and activity, and this opens the way to new investigations among more pathogenic viruses of the Phenuiviridae family.

ACS Style

Gianni Gori Savellini; Luca Bini; Assunta Gagliardi; Gabriele Anichini; Claudia Gandolfo; Shibily Prathyumnan; Maria Cusi. Ubiquitin and Not Only Unfolded Domains Drives Toscana Virus Non-Structural NSs Protein Degradation. Viruses 2020, 12, 1153 .

AMA Style

Gianni Gori Savellini, Luca Bini, Assunta Gagliardi, Gabriele Anichini, Claudia Gandolfo, Shibily Prathyumnan, Maria Cusi. Ubiquitin and Not Only Unfolded Domains Drives Toscana Virus Non-Structural NSs Protein Degradation. Viruses. 2020; 12 (10):1153.

Chicago/Turabian Style

Gianni Gori Savellini; Luca Bini; Assunta Gagliardi; Gabriele Anichini; Claudia Gandolfo; Shibily Prathyumnan; Maria Cusi. 2020. "Ubiquitin and Not Only Unfolded Domains Drives Toscana Virus Non-Structural NSs Protein Degradation." Viruses 12, no. 10: 1153.

Journal article
Published: 03 February 2020 in Vaccines
Reads 0
Downloads 0

An increase in measles cases worldwide, with outbreaks, has been registered in the last few years, despite the availability of a safe and highly efficacious vaccine. In addition to an inadequate vaccination coverage, even in high-income European countries studies proved that some vaccinated people were also found seronegative years after vaccination, thus increasing the number of people susceptible to measles infection. In this study, we evaluated the immunization status and the seroprevalence of measles antibodies among 1092 healthy adults, either vaccinated or naturally infected, in order to investigate the persistence of anti-measles IgG. Among subjects who received two doses of measles vaccine, the neutralizing antibody titer tended to decline over time. In addition, data collected from a neutralization assay performed on 110 healthy vaccinated subjects suggested an inverse correlation between neutralizing antibody titers and the time elapsed between the two vaccinations, with a significant decline in the neutralizing titer when the interval between the two doses was ≥11 years. On the basis of these results, monitoring the serological status of the population 10–12 years after vaccination could be important both to limit the number of people who are potentially susceptible to measles, despite the high efficacy of MMR vaccine, and to recommend a booster vaccine for the seronegatives.

ACS Style

Gabriele Anichini; Claudia Gandolfo; Simonetta Fabrizi; Giovan Battista Miceli; Chiara Terrosi; Gianni Gori Savellini; Shibily Prathyumnan; Daniela Orsi; Giuseppe Battista; Maria Grazia Cusi. Seroprevalence to Measles Virus after Vaccination or Natural Infection in an Adult Population, in Italy. Vaccines 2020, 8, 66 .

AMA Style

Gabriele Anichini, Claudia Gandolfo, Simonetta Fabrizi, Giovan Battista Miceli, Chiara Terrosi, Gianni Gori Savellini, Shibily Prathyumnan, Daniela Orsi, Giuseppe Battista, Maria Grazia Cusi. Seroprevalence to Measles Virus after Vaccination or Natural Infection in an Adult Population, in Italy. Vaccines. 2020; 8 (1):66.

Chicago/Turabian Style

Gabriele Anichini; Claudia Gandolfo; Simonetta Fabrizi; Giovan Battista Miceli; Chiara Terrosi; Gianni Gori Savellini; Shibily Prathyumnan; Daniela Orsi; Giuseppe Battista; Maria Grazia Cusi. 2020. "Seroprevalence to Measles Virus after Vaccination or Natural Infection in an Adult Population, in Italy." Vaccines 8, no. 1: 66.

Research article
Published: 09 December 2019 in PLOS Pathogens
Reads 0
Downloads 0

It is known that the non-structural protein (NSs) of Toscana virus (TOSV), an emergent sandfly-borne virus causing meningitis or more severe central nervous system injuries in humans, exerts its function triggering RIG-I for degradation in a proteasome-dependent manner, thus breaking off the IFN-β production. The non-structural protein of different members of Bunyavirales has recently appeared as a fundamental protagonist in immunity evasion through ubiquitination-mediated protein degradation targets. We showed that TOSV NSs has an E3 ubiquitin ligase activity, mapping at the carboxy-terminal domain and also involving the amino-terminal of the protein. Indeed, neither the amino- (NSsΔN) nor the carboxy- (NSsΔC) terminal-deleted mutants of TOSV NSs were able to cause ubiquitin-mediated proteasome degradation of RIG-I. Moreover, the addition of the C-terminus of TOSV NSs to the homologous protein of the Sandfly Fever Naples Virus, belonging to the same genus and unable to inhibit IFN-β activity, conferred new properties to this protein, favoring RIG-I ubiquitination and its degradation. NSs lost its antagonistic activity to IFN when one of the terminal residues was missing. Therefore, we showed that NSs could behave as an atypical RING between RING (RBR) E3 ubiquitin ligases. This is the first report which identified the E3 ubiquitin ligase activity in a viral protein among negative strand RNA viruses. Toscana virus is an emergent sandfly-borne virus mainly transmitted to humans by phlebotomine sandflies, which can cause meningitis or more severe central nervous system injuries in some subjects. As many other RNA viruses, it counteracts IFN-β expression by its non-structural protein. Our results expanded our knowledge about the molecular mechanisms by which TOSV exerts its activity as an E3 ubiquitin ligase. This is the first example of a viral protein presenting this activity among negative-strand RNA viruses. Thus, the recognition of this activity and its substrates among viruses are of primary importance to understand how viruses can alter their fitness by the ubiquitin pathway and provide an attractive target for the development of antiviral therapies.

ACS Style

Gianni Gori Savellini; Gabriele Anichini; Claudia Gandolfo; Shibily Prathyumnan; Maria Grazia Cusi. Toscana virus non-structural protein NSs acts as E3 ubiquitin ligase promoting RIG-I degradation. PLOS Pathogens 2019, 15, e1008186 .

AMA Style

Gianni Gori Savellini, Gabriele Anichini, Claudia Gandolfo, Shibily Prathyumnan, Maria Grazia Cusi. Toscana virus non-structural protein NSs acts as E3 ubiquitin ligase promoting RIG-I degradation. PLOS Pathogens. 2019; 15 (12):e1008186.

Chicago/Turabian Style

Gianni Gori Savellini; Gabriele Anichini; Claudia Gandolfo; Shibily Prathyumnan; Maria Grazia Cusi. 2019. "Toscana virus non-structural protein NSs acts as E3 ubiquitin ligase promoting RIG-I degradation." PLOS Pathogens 15, no. 12: e1008186.