Doliana, Roberto

Link to this page

Authority KeyName Variants
bb9f720e-4635-4c63-846f-d165e45603a5
  • Doliana, Roberto (1)
Projects
No records found.

Author's Bibliography

EMILINs Interact with Anthrax Protective Antigen and Inhibit Toxin Action in Vitro

Doliana, Roberto; Veljković, Veljko; Prljić, Jelena; Veljković, Nevena V.; De Lorenzo, Elisa; Mongiat, Maurizio; Ligresti, Giovanni; Marastoni, Stefano; Colombatti, Alfonso

(2008)

TY  - JOUR
AU  - Doliana, Roberto
AU  - Veljković, Veljko
AU  - Prljić, Jelena
AU  - Veljković, Nevena V.
AU  - De Lorenzo, Elisa
AU  - Mongiat, Maurizio
AU  - Ligresti, Giovanni
AU  - Marastoni, Stefano
AU  - Colombatti, Alfonso
PY  - 2008
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/3377
AB  - The informational spectrum method (ISM) is a virtual spectroscopy method for the fast analysis of potential protein-protein relationships. By applying the ISM approach to the GeneBank protein database the vascular proteins EMILIN1 (Elastin Microfibril Interface Located ProteIN), EMILIN2, MMN1, and MMN2 were identified as additional anthrax PA antigen interacting molecules. This virtual molecular interaction was formally proven by solid phase assays using recombinant proteins. The interaction is independent of the presence of divalent cations and does not involve PA aspartic residue at 683, a critical residue in receptor binding. In fact, the D683A point mutation fully prevented the cell intoxication ability of PA in the presence of Lethal Factor, but it was fully ineffective on the binding of mutated PA to EMILIN1 and EMILIN2. The ISM approach also led to the identification of the potential interaction sites between PA and EMILINs. A PA mutant with a deletion at residue D425 and solid phase protein-protein interaction studies as well as deletion mutant of EMILIN2 confirmed the hypothesized interaction site. Our findings imply that the PA-cell surface receptor interaction is not likely to provide the full explanation for the vascular lesions and prominent hemorrhages that follow Bacillus anthracis infection and spreading and call into play vascular associated proteins such as EMILINs as potential inhibitory proteins. (c) 2007 Elsevier B.V/International Society of Matrix Biology. All rights reserved.
T2  - Matrix Biology
T1  - EMILINs Interact with Anthrax Protective Antigen and Inhibit Toxin Action in Vitro
VL  - 27
IS  - 2
SP  - 96
EP  - 106
DO  - 10.1016/j.matbio.2007.09.008
ER  - 
@article{
author = "Doliana, Roberto and Veljković, Veljko and Prljić, Jelena and Veljković, Nevena V. and De Lorenzo, Elisa and Mongiat, Maurizio and Ligresti, Giovanni and Marastoni, Stefano and Colombatti, Alfonso",
year = "2008",
abstract = "The informational spectrum method (ISM) is a virtual spectroscopy method for the fast analysis of potential protein-protein relationships. By applying the ISM approach to the GeneBank protein database the vascular proteins EMILIN1 (Elastin Microfibril Interface Located ProteIN), EMILIN2, MMN1, and MMN2 were identified as additional anthrax PA antigen interacting molecules. This virtual molecular interaction was formally proven by solid phase assays using recombinant proteins. The interaction is independent of the presence of divalent cations and does not involve PA aspartic residue at 683, a critical residue in receptor binding. In fact, the D683A point mutation fully prevented the cell intoxication ability of PA in the presence of Lethal Factor, but it was fully ineffective on the binding of mutated PA to EMILIN1 and EMILIN2. The ISM approach also led to the identification of the potential interaction sites between PA and EMILINs. A PA mutant with a deletion at residue D425 and solid phase protein-protein interaction studies as well as deletion mutant of EMILIN2 confirmed the hypothesized interaction site. Our findings imply that the PA-cell surface receptor interaction is not likely to provide the full explanation for the vascular lesions and prominent hemorrhages that follow Bacillus anthracis infection and spreading and call into play vascular associated proteins such as EMILINs as potential inhibitory proteins. (c) 2007 Elsevier B.V/International Society of Matrix Biology. All rights reserved.",
journal = "Matrix Biology",
title = "EMILINs Interact with Anthrax Protective Antigen and Inhibit Toxin Action in Vitro",
volume = "27",
number = "2",
pages = "96-106",
doi = "10.1016/j.matbio.2007.09.008"
}
Doliana, R., Veljković, V., Prljić, J., Veljković, N. V., De Lorenzo, E., Mongiat, M., Ligresti, G., Marastoni, S.,& Colombatti, A.. (2008). EMILINs Interact with Anthrax Protective Antigen and Inhibit Toxin Action in Vitro. in Matrix Biology, 27(2), 96-106.
https://doi.org/10.1016/j.matbio.2007.09.008
Doliana R, Veljković V, Prljić J, Veljković NV, De Lorenzo E, Mongiat M, Ligresti G, Marastoni S, Colombatti A. EMILINs Interact with Anthrax Protective Antigen and Inhibit Toxin Action in Vitro. in Matrix Biology. 2008;27(2):96-106.
doi:10.1016/j.matbio.2007.09.008 .
Doliana, Roberto, Veljković, Veljko, Prljić, Jelena, Veljković, Nevena V., De Lorenzo, Elisa, Mongiat, Maurizio, Ligresti, Giovanni, Marastoni, Stefano, Colombatti, Alfonso, "EMILINs Interact with Anthrax Protective Antigen and Inhibit Toxin Action in Vitro" in Matrix Biology, 27, no. 2 (2008):96-106,
https://doi.org/10.1016/j.matbio.2007.09.008 . .
4
21
17
20