Maria Monti
Proteomica e proteomica clinica

Maria Monti

Principal Investigator

Associated Professor of Biochemistry

Supervisor CEINGE Criopreservation Facility and Proteomics Facility 

  • 1997: Degree in Chemistry at the University "Federico II" of Napoli.
  • 1998: Post-graduate fellow at the University "Federico II" of Napoli.
  • 1999 - 2000: Research Assistant of the Parco Scientifico e Tecnologico dell’Area Metropolitana di Napoli, at the CEINGE-Biotecnologie Avanzate s.c.a r. l.
  • 2000-2003: PhD in Biochemistry and Molecular Biology, University "Federico II" of Naples.
  • 2003: Visiting Scientist at the Department of Biomolecular Mass Spectrometry, Utrecht University, the Netherlands.
  • 2004-2006: Research Assistant at the CEINGE-Biotecnologie Avanzate s.c.a r. l.
  • 2006-2015: Research Assistant at the Department of Organic Chemistry and Biochemistry, University "Federico II" of Napoli.
  • Since October 2015: Assistant Professor of Biochemistry at the Department of Chemical Sciences, University "Federico II" of Naples.


Teaching activities: Professor of "Structural and Functional Proteomics" at Master Degree in Chemical Sciences and of "Advanced Biochemistry" at Bachelor Degree in Biomolecular and Industrial Biotechnologies of University "Federico II" of Naples.



The scientific activity of Prof. Maria Monti has always been addressed to the structural characterization of proteins using classical protein chemistry procedures in combination with advanced mass spectrometric methodologies. In particular, many studies have been focused on characterization of post-translational modifications (S-S bridges assignment, identification of glycosylation and S-glutathionylation sites, glycoforms analysis, epigenetic histones modifications, etc), and on the investigation of surface topology of protein-protein and protein-DNA complexes and of supra-molecular complexes, such as amyloid oligomers and fibrils, by employing a limited proteolysis approach and advanced mass spectrometric methodologies. More recently, studies have been addressed to the elucidation of the molecular mechanisms of biological processes both in physiological and pathological conditions, by investigating protein interactome, as well as by studying the alteration in proteome profiles of samples differently treated, by using different proteomics approaches.

Research lines
  1.  Investigation of protein trafficking alteration in Lysosomal Storage Diseases (LSDs)

Pompe and Fabry diseases (PD and FD) belong to lysosomal storage diseases (LSDs), rare inherited metabolic disorders.

PD and FD are associated with mutations in the GAA and GLA coding genes, respectively, resulting in lysosomal accumulation of glycogen in PD and globotriaosylceramide (Gb3) in FD. Many of the mutant proteins show defects in the traffic to lysosomes. These defects can be partially remedied by the administration of recombinant proteins. Therefore, to understand the molecular basis of these pathologies, we are studying the trafficking of the endogenous proteins and the internalized drugs, by using proteomic approaches.


  1.  Investigation of histone epigenetic modifications by using high resolution LC-MSMS approaches

The comprehension of histones epigenetic code is strictly connected with the identification and relative quantification of several post translational modifications (PTMs).

New protocols based on limited proteolysis and high resolution LC-MSMS methodologies have been developed to identify, localize and quantify the variations of these PTMs in specific experimental conditions.


  1.  Conformational analysis of protein complexes

Conformational studies of protein complexes with different ligands (proteins, oligonucleotides, metal ligands, lipids, etc.) are carried out by using direct ESI-MS analysis and limited proteolysis approaches, in order to obtain information on the stoichiometry of the complexes and on the binding modalities at molecular level.

Most relevant publications

1. Hoogenraad CC, Popa I, Futai K, Sanchez-Martinez E, Wulf PS, van Vlijmen T, Dortland BR, Oorschot V, Govers R, Monti M, Heck AJ, Sheng M, Klumperman J, Rehmann H, Jaarsma D, Kapitein LC, van der Sluijs P.

Neuron specific Rab4 effector GRASP-1 coordinates membrane specialization and maturation of recycling endosomes.

PLoS Biol. 2010, 8(1):e1000283          


2. D'Angelo G, Uemura T, Chuang CC, Polishchuk E, Santoro M, Ohvo-Rekilä H, Sato T, Di Tullio G, Varriale A, D'Auria S, Daniele T, Capuani F, Johannes L, Mattjus P, Monti M, Pucci P, Williams RL, Burke JE, Platt FM, Harada A, De Matteis MA.

Vesicular and non-vesicular transport feed distinct glycosylation pathways in the Golgi.

Nature 2013, 501(7465):116-20. doi: 10.1038/nature12423


3. Chesi G, Hegde RN, Iacobacci S, Concilli M, Parashuraman S, Festa BP, Polishchuk EV, Di Tullio G, Carissimo A, Montefusco S, Canetti D, Monti M, Amoresano A, Pucci P, van de Sluis B, Lutsenko S, Luini A, Polishchuk RS.

Identification of p38 MAPK and JNK as new targets for correction of Wilson disease-causing ATP7B mutants.

Hepatology, 2016, 63(6):1842-59. doi: 10.1002/hep.28398.


4. Zollo M., Ahmed M., Ferrucci V., Salpietro V., Asadzadeh F., Carotenuto M., Maroofian R., Al-Amri A., Singh R., Scognamiglio I., Mojarrad M., Musella L., Duilio A., Di Somma A., Karaca E., Rajab A., Al-Khayat A., Mohan Mohapatra T., Eslahi A., Ashrafzadeh F., Rawlins L. E., Prasad R., Gupta R., Kumari P., Srivastava M., Cozzolino F., Rai S. K., Monti M., Harlalka G. V., Simpson M. A., Rich P., AlSalmi F., Patton M. A.,. Chioza B. A, Efthymiou S., Granata F., Di Rosa G., Wiethoff S., Borgione E., Scuderi C., Mankad K.,. Hanna M. G., Pucci P., Houlden H., Lupski J.R., Crosby A. H. and Baple E. L.

PRUNE is crucial for normal brain development and mutated in microcephaly with neurodevelopmental impairment

Brain. 2017, 140(4):940-952. doi: 10.1093/brain/awx014


5. Zappa F, Wilson C, Di Tullio G, Santoro M, Pucci P, Monti M, D'Amico D, Pisonero-Vaquero S, De Cegli R, Romano A, Saleem MA, Polishchuk E, Failli M, Giaquinto L, De Matteis MA.

The TRAPP complex mediates secretion arrest induced by stress granule assembly.

EMBO J. 2019 Aug 20:e101704. doi: 10.15252/embj.2019101704.