Alessandra M. Martorana

ORCID: 0000-0003-3996-4141
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About
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Research Areas
  • Bacterial Genetics and Biotechnology
  • Antibiotic Resistance in Bacteria
  • RNA and protein synthesis mechanisms
  • Escherichia coli research studies
  • Bacteriophages and microbial interactions
  • Immune Response and Inflammation
  • Bacterial biofilms and quorum sensing
  • Carbohydrate Chemistry and Synthesis
  • Genomics and Phylogenetic Studies
  • Chemical Synthesis and Analysis
  • Advanced Proteomics Techniques and Applications
  • Cell Adhesion Molecules Research
  • biodegradable polymer synthesis and properties
  • Prion Diseases and Protein Misfolding
  • vaccines and immunoinformatics approaches
  • Legume Nitrogen Fixing Symbiosis
  • Antimicrobial Resistance in Staphylococcus
  • Biochemical Analysis and Sensing Techniques
  • Tuberculosis Research and Epidemiology
  • Machine Learning in Bioinformatics
  • Click Chemistry and Applications
  • Antimicrobial Peptides and Activities
  • Alzheimer's disease research and treatments
  • Clostridium difficile and Clostridium perfringens research
  • Vibrio bacteria research studies

University of Milan
2010-2025

University of Milano-Bicocca
2014-2017

In Gram-negative bacteria, the outer membrane protects cell against many toxic molecules, and peptidoglycan layer provides protection osmotic challenges, allowing bacterial cells to survive in changing environments. Maintaining envelope integrity is therefore a question of life or death for cell. Here we show that Escherichia coli activate LD-transpeptidase LdtD introduce 3-3 cross-links when compromised, this response required avoid lysis. This remodeling program strategy increase overall...

10.1128/mbio.02729-18 article EN cc-by mBio 2019-02-04

Lipopolysaccharide is a major glycolipid component in the outer leaflet of membrane (OM), peculiar permeability barrier Gram-negative bacteria that prevents many toxic compounds from entering cell. transport (Lpt) across periplasmic space and its assembly at Escherichia coli cell surface are carried out by transenvelope complex seven essential Lpt proteins spanning inner (LptBCFG), periplasm (LptA), OM (LptDE), which appears to operate as unique machinery. LptC an membrane-anchored protein...

10.1128/jb.02057-12 article EN Journal of Bacteriology 2013-01-04

Significance The antimicrobial effect of copper has been known since ancient times and it is well that alloy surfaces kill various disease-causing bacteria, fungi, viruses, preventing the spread antibiotic resistance through horizontal gene transfer between pathogens. However, there little knowledge about specific targets toxicity in bacteria. Here we show inhibits peptidoglycan LD-transpeptidases, causing higher permeability outermembrane precluding strains Escherichia coli Enterococcus...

10.1073/pnas.1809285115 article EN Proceedings of the National Academy of Sciences 2018-10-01

The outer membrane (OM) of Gram-negative bacteria is a highly selective permeability barrier due to its asymmetric structure with lipopolysaccharide (LPS) in the leaflet. In Escherichia coli, LPS transported cell surface by transport (Lpt) system composed seven essential proteins forming transenvelope bridge. Transport powered ABC transporter LptB2FGC, which extracts from inner (IM) and transfers it, through LptC protein, periplasmic protein LptA. Then, LptA delivers OM LptDE translocon for...

10.3389/fmicb.2020.00909 article EN cc-by Frontiers in Microbiology 2020-05-13

ABSTRACT Lipopolysaccharide (LPS) is a major glycolipid present in the outer membrane (OM) of Gram-negative bacteria. The peculiar permeability barrier OM due to presence LPS at leaflet this that prevents many toxic compounds from entering cell. In Escherichia coli synthesized inside cell first translocated over inner (IM) by essential MsbA flippase; then, seven Lpt proteins located IM (LptBCDF), periplasm (LptA), and (LptDE) are responsible for transport across periplasmic space its...

10.1128/jb.01037-10 article EN Journal of Bacteriology 2010-12-18

In Gram-negative bacteria, lipopolysaccharide (LPS) contributes to the robust permeability barrier of outer membrane (OM), preventing entry toxic molecules, such as detergents and antibiotics. LPS is transported from inner (IM) OM by Lpt multiprotein machinery. Defects in transport compromise assembly at result increased antibiotic sensitivity. LptA a key component machine that interacts with IM protein LptC chaperones through periplasm. We report here construction lptA41, quadruple mutant...

10.1128/jb.00487-17 article EN Journal of Bacteriology 2017-11-06

The integrity of the cell envelope E. coli relies on concerted activity multi-protein machineries that synthesize peptidoglycan (PG) and outer membrane (OM). Our previous work found depletion lipopolysaccharide (LPS) export to OM induces an essential PG remodeling process involving LD-transpeptidases (LDTs), glycosyltransferase function PBP1B carboxypeptidase PBP6a. Consequently, cells with defective biogenesis lyse if they lack any these enzymes. Here we report morphological defects, lysis...

10.1111/mmi.14712 article EN cc-by Molecular Microbiology 2021-03-04

Lipopolysaccharide (LPS) is an essential structural component of the outer membrane (OM) most Gram-negative bacteria. In model organism Escherichia coli, LPS transport to OM requires seven proteins (LptABCDEFG) that form a continuous bridge across cell envelope. Pseudomonas aeruginosa recently-demonstrated essentiality LptD and LptH, P. LptA homologue, confirmed crucial role Lpt system and, thus, in biogenesis this species. Surprisingly, independent high-throughput transposon mutagenesis...

10.1080/21505594.2018.1537730 article EN cc-by Virulence 2018-10-25

The cell envelope of Gram-negative bacteria is a complex multi-layered structure comprising an inner cytoplasmic membrane and additional asymmetric lipid bilayer, the outer membrane, which functions as selective permeability barrier essential for viability. Lipopolysaccharide, glycolipid located in leaflet greatly contributes to peculiar properties exhibited by membrane. This molecule transported surface molecular machine composed seven proteins LptABCDEFG that form transenvelope function...

10.1371/journal.pone.0100941 article EN cc-by PLoS ONE 2014-06-26

Lipopolysaccharide (LPS) is the main glycolipid present in outer leaflet of membrane (OM) Gram-negative bacteria, where it modulates OM permeability, therefore preventing many toxic compounds from entering cell. LPS biogenesis an essential process bacteria and thus ideal target pathway for development novel specific antimicrobials. The lipopolysaccharide transport (Lpt) system responsible transporting periplasmic surface inner membrane, assembled, to cell then inserted OM. Lpt has been...

10.1111/febs.13254 article EN FEBS Journal 2015-03-04

ABSTRACT Peptidoglycan hydrolases facilitate bacterial cell wall growth by creating space for insertion of new material and allowing physical separation daughter cells. In Escherichia coli , three peptidoglycan amidases, AmiA, AmiB AmiC, cleave septal during division. The LytM-domain proteins EnvC NlpD activate these amidases either from inside the or outer membrane: binds to cytoplasmic membrane-anchored divisome components FtsEX, ActS are membrane lipoproteins. Here we report...

10.1101/2025.02.18.638797 preprint EN cc-by bioRxiv (Cold Spring Harbor Laboratory) 2025-02-19

Nuclear factor of activated T cells (NFAT) is in innate immune downstream pattern recognition receptors, but little known about NFAT's functions immunity compared with adaptive immunity. We show that early activation NFAT balances the two major phases response to Candida albicans skin infections: protective containment (abscess) and elimination (expulsion) phases. During phase, transforming growth factor-β (TGF-β) induces deposit collagen around newly recruited polymorphonuclear prevent...

10.1126/sciimmunol.aan2725 article EN Science Immunology 2017-09-01

Lipopolysaccharides (LPS) are complex glycolipids forming the outside layer of Gram-negative bacteria. Their hydrophobic and heterogeneous nature greatly hampers their structural study in an environment similar to bacterial surface. We have studied LPS purified from E. coli pathogenic P. aeruginosa with long O-antigen polysaccharides assembled solution as vesicles or elongated micelles. Solid-state NMR magic-angle spinning permitted identification signals arising regions different...

10.1021/acschembio.8b00271 article EN ACS Chemical Biology 2018-07-02

Gram-negative bacteria have a unique cell envelope with lipopolysaccharide-containing outer membrane that is tightly connected to thin layer of peptidoglycan. The tight connection between the and peptidoglycan needed maintain as an impermeable barrier for many toxic molecules antibiotics. Enterobacteriaceae such Escherichia coli covalently attach abundant membrane-anchored lipoprotein Lpp (Braun's lipoprotein) tripeptides in peptidoglycan, mediated by transpeptidases LdtA, LdtB, LdtC. LdtD...

10.1128/mbio.00836-21 article EN cc-by mBio 2021-05-10

The assembly of lipopolysaccharide (LPS) in the outer leaflet membrane (OM) requires transenvelope Lpt (lipopolysaccharide transport) complex, made Escherichia coli seven essential proteins located inner (IM) (LptBCFG), periplasm (LptA), and OM (LptDE). At IM, LptBFG constitute an unusual ATP binding cassette (ABC) transporter, composed by transmembrane LptFG cytoplasmic LptB ATPase, which is thought to extract LPS from IM provide energy for its export across cell surface. LptC a small...

10.1128/jb.00329-16 article EN Journal of Bacteriology 2016-06-01

Background: Pseudomonas aeruginosa cell envelope-associated proteins play a relevant role in infection mechanisms. They can contribute to the antibiotic resistance of bacterial cells and be involved interaction with host cells. Thus, studies contributing elucidating these key molecular elements are great importance find alternative therapeutics. Methods: Proteins peptides were extracted by different methods analyzed Multidimensional Protein Identification Technology (MudPIT) approach....

10.3390/cells9112421 article EN cc-by Cells 2020-11-05

Abstract Oligomeric and fibrillar aggregates generated by amyloid‐β (Aβ) prion protein (PrP) peptides are amongst the principal components of amyloid plaques found post mortem in patients suffering from Alzheimer’s disease mammalian diseases. Hence these represent major molecular targets to develop potential drugs diagnostic tools for above‐mentioned neurodegenerative Recently, a small library cis ‐glyco‐fused benzopyran compounds has been synthesized us, their ability recognize bind Aβ...

10.1002/cplu.201400035 article EN ChemPlusChem 2014-06-01

Abstract We synthesized a small library of N‐ spirofused bicyclic derivatives 1‐deoxynojirimycin (DNJ), as quaternary ammonium salts, through double S N 2 annulation process. The rings are different size and structural characteristics. Preliminary biological evaluation showed no antibacterial activity towards both Gram+ Gram‐ bacteria. DNJ derivative bearing 6 member cycle revealed promising inhibitor amyloglucosidase. Binding energies calculated docking studies resembled the in vitro...

10.1002/slct.201600516 article EN ChemistrySelect 2016-07-01
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