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Table I.
Overview of the inactivation methods used to inactivate PRRSV.
Method | Type | Mechanism |
---|---|---|
Formaldehyde | Alkylating agent | Monohydroxy-methylizing of adenine [1] |
Cross-linker | Cross-linking of RNA to capsid proteins [20, 27, 32], causing a block of genome reading [49] | |
Cross-linking of proteins by formation of inter- and intramolecular methylene bridges between hydroxymethylated amines [22] | ||
Glutaraldehyde | Cross-linker | Cross-linking of proteins by the same mechanism as formaldehyde described above [8] |
AT-2 | Cross-linker | Cross-linking of proteins by oxidation of S-H groups causing formation of S-S bridges which results in a covalent modification and functional inactivation of S-H-containing internal viral proteins [7] |
pH | Denaturation agent | Denaturation of proteins, the conformation of spike proteins of coronaviruses for example enables fusion of the virus with the host cell by changes to a pH of 8 [62] |
Temperature | Denaturation agent | A high temperature denaturates proteins. As a result, the conformation of viral proteins that are involved in attachment and replication in a host cell may have changed [31, 56] |
Gamma irradiation | Radiation | Viruses are inactivated primarily by direct damage, via disruption of the genome [24] |
Formation of free radicals which damage proteins [24] | ||
UV light | Radiation | Induction of dimer formation between adjacent uracils in RNA [40, 57]. Dimer formation leads to pressure and breakage of the sugar backbone causing a block of genome reading |
More slowly, UV also causes structural modifications of the capsid proteins resulting in the formation of large and small photoproducts [40, 58] | ||
BEI | Alkylating agent | Alkylation of RNA at low concentrations. Most likely genome reading is blocked by alkylation of guanine or adenine by BEI [4, 23] |
Alkylation of proteins (nucleocapsid) at high concentrations [4] |