Comparative study of antibody titers induced by synthetic peptides belonging to VP2 and VP3 capsid proteins of hepatitis A virus

Pérez, José; Mota, Felipe Machado; González-Dankaart, Juan F.; Pintó, Rosa M.; Bosch, Alexandre; Reig, F.; Haro, Isabel

doi:10.1007/978-94-011-1468-4_377

Cited by 8 publications

(9 citation statements)

References 4 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In the search for a synthetic vaccine effective against hep-Our main objectives were, first, to find the optimal liposome atitis A, different peptides derived from the VP1 capsid pro-composition that ensures maximal peptide entrapment, in tein of hepatitis A virus (HAV) have been synthesized and order to prepare a synthetic hepatitis A vaccine based on some of them have shown the ability to elicit the production liposomes and, second, to better understand the interaction of of virus-neutralizing and protective antibodies (1,2). Pep-the antigen with the lipid membrane.…”

Section: Introductionmentioning

confidence: 99%

Interaction of a Multiple Antigenic Peptide of Hepatitis A Virus with Monolayers and Bilayers of Acidic, Basic, and Zwitterionic Phospholipids

Cajal

Alsina

Reig

et al. 1998

Journal of Colloid and Interface Science

Self Cite

View full text Add to dashboard Cite

Section: Introductionmentioning

confidence: 99%

Interaction of a Multiple Antigenic Peptide of Hepatitis A Virus with Monolayers and Bilayers of Acidic, Basic, and Zwitterionic Phospholipids

Cajal

Alsina

Reig

et al. 1998

Journal of Colloid and Interface Science

Self Cite

View full text Add to dashboard Cite

“…VP3(110–121) was obtained manually on a Wang resin (functionalization 0.8 meq/g), by means of an diisopropilcarbodiimide/hidroxybenzotriazole activation as previously described 21…”

Section: Methodsmentioning

confidence: 99%

Effect of chain length of HAV-VP3 synthetic peptides on its interaction with biomembrane models

Sospedra¹,

Muñoz²,

García³

et al. 2000

Biopolymers

Self Cite

View full text Add to dashboard Cite

Shorter analogues of a continuous epitope of hepatitis A virus, VP3(110–121) peptide, failed to react with convalescent sera, indicating the importance of the entire peptide in the epitope structure. To better understand the influence of the structural properties of this 12‐mer peptide epitope on its biological activity, the interaction of smaller peptide analogues with phospholipid biomembrane models was investigated by a combination of spectroscopic and biophysical techniques. In this article we describe our findings concerning the surface activity and the interaction of peptides with simple mono‐ and bilayer membranes composed of a zwitterionic phospholipid (dipalmitoyl phosphatidylcholine, DPPC), an anionic phospholipid (dipalmitoyl phosphatidylglicerol, DPPG), or a DPPC/DPPG mixture. The results indicate that the net negative charge of the peptide is in some way responsible of the specific interactions between VP3(110–121) and membrane phospholipids, and necessary to induce β‐type conformations upon vesicle interaction. © 2000 John Wiley & Sons, Inc. Biopoly 54: 477–488, 2000

show abstract

“…MAP 4 VP3(110 -121) was synthesized, purified, and characterized as described elsewhere 16 ; its purity was Ͼ99%. 1,6-Diphenyl-1,3,5-hexatriene (DPH), carboxyfluorescein (CF), and dithionite (sodium hypodisulfite) were from Fluka.…”

Section: Methodsmentioning

confidence: 99%

Fluorescence study on the interaction of a multiple antigenic peptide from hepatitis A virus with lipid vesicles

Ortiz¹,

Cajal²,

Haro³

et al. 2000

Biopolymers

Self Cite

View full text Add to dashboard Cite

The interaction of the multiple antigenic peptide MAP4VP3 with lipid membranes has been studied by spectroscopic techniques. MAP4VP3 is a multimeric peptide that corresponds to four units of the sequence 110-121 of the capsid protein VP3 of hepatitis A virus. In order to evaluate the electrostatic and hydrophobic components on the lipid-peptide interaction, small unilamelar vesicles of different compositions, including zwitterionic dipalmitoylphosphatidylcholine (DPPC), anionic dipalmitoylphosphatidylcholine/phatidylinositol (DPPC:PI 9:1), and cationic dipalmitoylphosphatidylcholine/stearylamine (DPPC:SA 9.5:0.5), were used as membrane models. Intrinsic tryptophan fluorescence changes and energy transfer experiments show that MAP4VP3 binds to all three types of vesicles with the same stoichiometry, indicating that the electrostatic component of the interaction is not important for binding of this anionic peptide. Steady-state polarization experiments with vesicles labeled with 1,6-diphenyl-1,3,5-hexatriene or with 1-anilino-8-naphtalene sulphonic acid indicate that MAP4VP3 induces a change in the packing of the bilayers, with a decrease in the fluidity of the lipids and an increase in the temperature of phase transition in all the vesicles. The percentage of lipid exposed to the bulk aqueous phase is around 60% in intact vesicles, and it does not change upon binding of MAP4VP3 to DPPC vesicles, indicating that the peptide does not alter the permeability of the membrane. An increase in the amount of lipid exposed to the aqueous phase in cationic vesicles indicates either lipid flip-flop or disruption of the vesicles. Binding to DPPC vesicles occurs without leakage of entrapped carboxyfluorescein, even at high mol fractions of peptide. However, a time-dependent leakage is seen with cationic DPPC/SA and anionic DPPC/PI vesicles, indicating that the peptide induces membrane destabilization and not lipid flip-flop. Resonance energy transfer experiments show that MAP4VP3 leakage from cationic vesicles is due to membrane fusion, whereas leakage from anionic vesicles is not accompanied by lipid mixing. Results show that MAP4VP3 interacts strongly with the lipid components of the membrane, and although binding is not of electrostatic nature, the bound form of the peptide has different activity depending on the membrane net charge; thus, it is membrane disruptive in cationic and anionic vesicles, whereas no destabilizing effect is seen in DPPC vesicles.

show abstract

Comparative study of antibody titers induced by synthetic peptides belonging to VP2 and VP3 capsid proteins of hepatitis A virus

Cited by 8 publications

References 4 publications

Interaction of a Multiple Antigenic Peptide of Hepatitis A Virus with Monolayers and Bilayers of Acidic, Basic, and Zwitterionic Phospholipids

Interaction of a Multiple Antigenic Peptide of Hepatitis A Virus with Monolayers and Bilayers of Acidic, Basic, and Zwitterionic Phospholipids

Effect of chain length of HAV-VP3 synthetic peptides on its interaction with biomembrane models

Fluorescence study on the interaction of a multiple antigenic peptide from hepatitis A virus with lipid vesicles

Contact Info

Product

Resources

About