The antiviral activity of naturally occurring proteins and their peptide fragments after chemical modification
Identifieur interne : 001108 ( Main/Exploration ); précédent : 001107; suivant : 001109The antiviral activity of naturally occurring proteins and their peptide fragments after chemical modification
Auteurs : Anna Oevermann [Suisse] ; Monika Engels [Suisse] ; Ursula Thomas [Suisse] ; Antonio Pellegrini [Suisse]Source :
- Antiviral research [ 0166-3542 ] ; 2003.
Descripteurs français
- KwdFr :
- Albumines (), Albumines (pharmacologie), Anhydrides phtaliques (), Animaux, Antiviraux (), Antiviraux (pharmacologie), Cellules Vero, Chymotrypsine (), Effet cytopathogène viral, Fragments peptidiques (), Fragments peptidiques (pharmacologie), Herpèsvirus humain de type 1 (), Humains, Hydrolyse, Indicateurs et réactifs, Lactalbumine (), Lactalbumine (pharmacologie), Lysozyme (), Lysozyme (pharmacologie), Pepsine A (), Protéines (), Protéines (pharmacologie), Rouge neutre, Survie cellulaire (), Trypsine ().
- MESH :
- pharmacologie : Albumines, Antiviraux, Fragments peptidiques, Lactalbumine, Lysozyme, Protéines.
- Pascal (Inist)
- Albumines, Anhydrides phtaliques, Animaux, Antiviraux, Cellules Vero, Chymotrypsine, Effet cytopathogène viral, Fragments peptidiques, Herpèsvirus humain de type 1, Humains, Hydrolyse, Indicateurs et réactifs, Lactalbumine, Lysozyme, Pepsine A, Protéine, Fragment peptidique, Modification chimique, Antiviral, Composé naturel, Protéines, Protéolyse, Activité biologique, Herpesvirus hominis 1, Enzyme, Lysozyme, Rouge neutre, Survie cellulaire, Trypsine, β-Lactoglobuline.
- Wicri :
- topic : Enzyme.
English descriptors
- KwdEn :
- Albumins (chemistry), Albumins (pharmacology), Animals, Antiviral, Antiviral Agents (chemistry), Antiviral Agents (pharmacology), Biological activity, Cell Survival (drug effects), Chemical modification, Chlorocebus aethiops, Chymotrypsin (chemistry), Cytopathogenic Effect, Viral, Enzyme, Herpesvirus 1, Human (drug effects), Herpesvirus hominis 1, Humans, Hydrolysis, Indicators and Reagents, Lactalbumin, Lactalbumin (chemistry), Lactalbumin (pharmacology), Lysozyme, Muramidase (chemistry), Muramidase (pharmacology), Natural compound, Neutral Red, Pepsin A (chemistry), Peptide Fragments (chemistry), Peptide Fragments (pharmacology), Peptide fragment, Phthalic Anhydrides (chemistry), Protein, Proteins (chemistry), Proteins (pharmacology), Proteolysis, Trypsin (chemistry), Vero Cells.
- MESH :
- chemical , chemistry : Albumins, Antiviral Agents, Chymotrypsin, Lactalbumin, Muramidase, Pepsin A, Peptide Fragments, Phthalic Anhydrides, Proteins, Trypsin.
- chemical , pharmacology : Albumins, Antiviral Agents, Lactalbumin, Muramidase, Peptide Fragments, Proteins.
- drug effects : Cell Survival, Herpesvirus 1, Human.
- Animals, Chlorocebus aethiops, Cytopathogenic Effect, Viral, Humans, Hydrolysis, Indicators and Reagents, Neutral Red, Vero Cells.
Abstract
Chemical modification of the proteins bovine serum albumin, α-lactalbumin, β-lactoglobulin and chicken lysozyme by 3-hydroxyphthalic anhydride (3-HP) yielded compounds which exerted antiviral activity in vitro as compared with the native unmodified proteins. Of the three enveloped viruses tested, human herpes simplex virus type 1 (HSV-1), bovine parainfluenza virus type 3 and porcine respiratory corona virus, only HSV-1 proved sensitive to the 3-HP-proteins. All of the chemically modified proteins presented antiviral activity against HSV-1 when assayed before, during or after infection. However, to achieve HSV-1 inhibition, significantly higher concentrations of the modified proteins were required if present before infection as compared to during or after infection. Our results suggest that multiple mechanisms are involved in the inhibition of HSV-1 infection. Proteolytical digestion of albumin, α-lactalbumin, β-lactoglobulin and lysozyme by trypsin, chymotrypsin and pepsin yielded several peptide fragments with antiherpetic activity. Chemical modification of these peptide fragments by 3-HP generated peptides with antiviral activity, however, this was almost always combined with a cytotoxic effect on the Vero cells. Overall, our results suggest that targeted chemical modification of some natural products might provide compounds effective against HSV-1 infection.
Affiliations:
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Le document en format XML
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Albumins (chemistry)</term>
<term>Albumins (pharmacology)</term>
<term>Animals</term>
<term>Antiviral</term>
<term>Antiviral Agents (chemistry)</term>
<term>Antiviral Agents (pharmacology)</term>
<term>Biological activity</term>
<term>Cell Survival (drug effects)</term>
<term>Chemical modification</term>
<term>Chlorocebus aethiops</term>
<term>Chymotrypsin (chemistry)</term>
<term>Cytopathogenic Effect, Viral</term>
<term>Enzyme</term>
<term>Herpesvirus 1, Human (drug effects)</term>
<term>Herpesvirus hominis 1</term>
<term>Humans</term>
<term>Hydrolysis</term>
<term>Indicators and Reagents</term>
<term>Lactalbumin</term>
<term>Lactalbumin (chemistry)</term>
<term>Lactalbumin (pharmacology)</term>
<term>Lysozyme</term>
<term>Muramidase (chemistry)</term>
<term>Muramidase (pharmacology)</term>
<term>Natural compound</term>
<term>Neutral Red</term>
<term>Pepsin A (chemistry)</term>
<term>Peptide Fragments (chemistry)</term>
<term>Peptide Fragments (pharmacology)</term>
<term>Peptide fragment</term>
<term>Phthalic Anhydrides (chemistry)</term>
<term>Protein</term>
<term>Proteins (chemistry)</term>
<term>Proteins (pharmacology)</term>
<term>Proteolysis</term>
<term>Trypsin (chemistry)</term>
<term>Vero Cells</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Albumines ()</term>
<term>Albumines (pharmacologie)</term>
<term>Anhydrides phtaliques ()</term>
<term>Animaux</term>
<term>Antiviraux ()</term>
<term>Antiviraux (pharmacologie)</term>
<term>Cellules Vero</term>
<term>Chymotrypsine ()</term>
<term>Effet cytopathogène viral</term>
<term>Fragments peptidiques ()</term>
<term>Fragments peptidiques (pharmacologie)</term>
<term>Herpèsvirus humain de type 1 ()</term>
<term>Humains</term>
<term>Hydrolyse</term>
<term>Indicateurs et réactifs</term>
<term>Lactalbumine ()</term>
<term>Lactalbumine (pharmacologie)</term>
<term>Lysozyme ()</term>
<term>Lysozyme (pharmacologie)</term>
<term>Pepsine A ()</term>
<term>Protéines ()</term>
<term>Protéines (pharmacologie)</term>
<term>Rouge neutre</term>
<term>Survie cellulaire ()</term>
<term>Trypsine ()</term>
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<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Albumins</term>
<term>Antiviral Agents</term>
<term>Chymotrypsin</term>
<term>Lactalbumin</term>
<term>Muramidase</term>
<term>Pepsin A</term>
<term>Peptide Fragments</term>
<term>Phthalic Anhydrides</term>
<term>Proteins</term>
<term>Trypsin</term>
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<keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Albumins</term>
<term>Antiviral Agents</term>
<term>Lactalbumin</term>
<term>Muramidase</term>
<term>Peptide Fragments</term>
<term>Proteins</term>
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<keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Cell Survival</term>
<term>Herpesvirus 1, Human</term>
</keywords>
<keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Albumines</term>
<term>Antiviraux</term>
<term>Fragments peptidiques</term>
<term>Lactalbumine</term>
<term>Lysozyme</term>
<term>Protéines</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Animals</term>
<term>Chlorocebus aethiops</term>
<term>Cytopathogenic Effect, Viral</term>
<term>Humans</term>
<term>Hydrolysis</term>
<term>Indicators and Reagents</term>
<term>Neutral Red</term>
<term>Vero Cells</term>
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<keywords scheme="Pascal" xml:lang="fr"><term>Albumines</term>
<term>Anhydrides phtaliques</term>
<term>Animaux</term>
<term>Antiviraux</term>
<term>Cellules Vero</term>
<term>Chymotrypsine</term>
<term>Effet cytopathogène viral</term>
<term>Fragments peptidiques</term>
<term>Herpèsvirus humain de type 1</term>
<term>Humains</term>
<term>Hydrolyse</term>
<term>Indicateurs et réactifs</term>
<term>Lactalbumine</term>
<term>Lysozyme</term>
<term>Pepsine A</term>
<term>Protéine</term>
<term>Fragment peptidique</term>
<term>Modification chimique</term>
<term>Antiviral</term>
<term>Composé naturel</term>
<term>Protéines</term>
<term>Protéolyse</term>
<term>Activité biologique</term>
<term>Herpesvirus hominis 1</term>
<term>Enzyme</term>
<term>Lysozyme</term>
<term>Rouge neutre</term>
<term>Survie cellulaire</term>
<term>Trypsine</term>
<term>β-Lactoglobuline</term>
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<front><div type="abstract" xml:lang="en">Chemical modification of the proteins bovine serum albumin, α-lactalbumin, β-lactoglobulin and chicken lysozyme by 3-hydroxyphthalic anhydride (3-HP) yielded compounds which exerted antiviral activity in vitro as compared with the native unmodified proteins. Of the three enveloped viruses tested, human herpes simplex virus type 1 (HSV-1), bovine parainfluenza virus type 3 and porcine respiratory corona virus, only HSV-1 proved sensitive to the 3-HP-proteins. All of the chemically modified proteins presented antiviral activity against HSV-1 when assayed before, during or after infection. However, to achieve HSV-1 inhibition, significantly higher concentrations of the modified proteins were required if present before infection as compared to during or after infection. Our results suggest that multiple mechanisms are involved in the inhibition of HSV-1 infection. Proteolytical digestion of albumin, α-lactalbumin, β-lactoglobulin and lysozyme by trypsin, chymotrypsin and pepsin yielded several peptide fragments with antiherpetic activity. Chemical modification of these peptide fragments by 3-HP generated peptides with antiviral activity, however, this was almost always combined with a cytotoxic effect on the Vero cells. Overall, our results suggest that targeted chemical modification of some natural products might provide compounds effective against HSV-1 infection.</div>
</front>
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<affiliations><list><country><li>Suisse</li>
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<region><li>Canton de Zurich</li>
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<tree><country name="Suisse"><region name="Canton de Zurich"><name sortKey="Oevermann, Anna" sort="Oevermann, Anna" uniqKey="Oevermann A" first="Anna" last="Oevermann">Anna Oevermann</name>
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<name sortKey="Engels, Monika" sort="Engels, Monika" uniqKey="Engels M" first="Monika" last="Engels">Monika Engels</name>
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