Applied Microbiology: Open Access
Open Access
ISSN: 2471-9315
+44 1300 500008
ISSN: 2471-9315
+44 1300 500008
Viviana Izzo , Federica De Lise, Francesca Mensitieri, Fabrizio Dal Piaz, Eugenio Notomista, Giulia Rusciano, Antonio Sasso, Armando Zarrelli , Stefany Castaldi, Maria Lumacone, Amelia Filippelli , Alberto Di Do nato
Department of Biology, University of Federico II Naples, Italy
Department of Medicine, Surgery and Dentistry, University of Salerno, Italy
Department of Physics, University of Federico II Naples, Italy
Department of Chemistry, University of Federico II Naples, Italy
Scientific Tracks Abstracts: Appli Microbiol Open Access
Outer membrane vesicles (OMVs) are nanoscale proteoliposomes of 20-200 nm diameter, derived from the surface of many
gram- negative and gram-positive bacteria as part of their natural growth cycle. Natural OMVs have several important roles;
for example, they can contribute to bacterial survival by reducing levels of toxic compounds, removing stress products from the
cell such as misfolded periplasmic proteins, or are involved in biofilm formation. Interest in these bioparticles has grown over
the years, leading to important highlights concerning their composition, production, and their role in cellular communication
and environmental adaptation. In this context, an appealing source of OMVs can be retrieved in Novosphingobium sp. PP1Y, a
marine microorganism isolated in a polluted area of the harbor of Pozzuoli (Naples, Italy) and microbiologically characterized
by our research group. This bacterium is a non-pathogenic microorganism belonging to the order Sphingomonadales, which is
endowed with the ability to grow on a wide array of mono- and polycyclic aromatic compounds (PAHs) used as sole carbon and
energy source. N. sp. PP1Y genome has been sequenced and completely annotated, showing the presence of a complex metabolic
pattern, responsible for its growth in harsh environmental conditions. The growth of strain PP1Y shows the presence of an
equilibrium between a sessile and a planktonic form. We have successfully isolated OMVs from N. sp. PP1Y grown in minimal
medium supplemented with 0.4% glutamate as sole carbon and energy source (Fig.1). AFM, DLS and Nanosize analysis on
purified vesicles showed that N. sp. PP1Y OMVs have a circular morphology with a diameter of � 200 nm and are uniform in size
and shape, in accordance with other OMVs described in literature. Proteomic and fatty acid analysis suggested a specific protein
and fatty acid fingerprint of these extracellular nanostructures; in particular, among all proteins identified in OMVs, Protease IV
resulted to be the more abundant. Preliminary analysis showed that Protease IV is present in OMVs from strain PP1Y in its active
form, thus paving the way to the use of these structures as vehicles of specific enzymatic activities of biotechnological importance.
Recent Publications:
1. De Lise F, Mensitieri F, Tarallo V, Ventimiglia N, Vinciguerra R, Tramice A, Marchetti R, Pizzo E, Notomista E, Cafaro V,
Molinaro A, Birolo L, Di Donato A, Izzo V (2016) RHA-P: isolation, expression and characterization of a bacterial a-Lrhamnosidase
from Novosphingobium sp. PP1Y. J. Mol. Catal. B: Enzym 134, 136-147.
2. Donadio G, Sarcinelli C, Pizzo E, Notomista E, Pezzella A, Di Cristo C, De Lise F, Di Donato A, Izzo V (2015) The Toluene
o-Xylene Monooxygenase Enzymatic Activity for the Biosynthesis of Aromatic Antioxidants. PLoS One 10 (4), e0124427. doi:
10.1371/journal.pone.0124427.
3. D�Argenio V, Notomista E, Petrillo M, Cantiello P, Cafaro V, Izzo V, Naso B, Cozzuto L, Durante L, Troncone L, Paolella G,
Salvatore F, Di Donato A (2014) Complete sequencing of Novosphingobium sp. PP1Y reveals a biotechnologically meaningful
metabolic pattern. BMC Genomics 15:384.
4. Izzo V, Tedesco P, Notomista E, Pagnotta E, Di Donato A, Trincone A, Tramice A (2014) �±-Rhamnosidase activity in the
marine isolate Novosphingobium sp. PP1Y and its use in the bioconversion of flavonoids. J. Mol. Catal. B: Enzym. 105, 95-103.