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Feline infectious peritonitis (FIP) is associated with mutations in thefeline coronavirus (FCoV) genome that are thought to convert the subclinicalfeline enteric coronavirus (FECV) into the lethal feline infectious peritonitisvirus (FIPV). A key feature of FIPV, not shared with FECV, is the productiveinfection of macrophages. Therefore mutations in proteins that govern celltropism, such as the spike glycoprotein, may play an important role in FIPprogression. In a prior study, involving a limited number of samples, we haveshown an association of FIP with mutations in the protease cleavage-activationsite located between the receptor-binding and fusion domains of the FCoV spike(S1/S2). Here, we extend these studies to investigate a larger sample set andto obtain a more refined analysis of the mutations at this S1/S2 site. Ourlarger data set more clearly shows that the mutations acquired by FIPV at S1/S2are also accompanied by additional mutations at a second proteasecleavage-activation site located in the fusion domain (S2'), adjacent to theviral fusion peptide. Overall, our data indicate a pattern of mutations acrossthe two protease recognition sites that results in substitutions, and/oraltered recognition, of critical basic/polar amino acid residues needed forvirus activation in the enteric tract. Typically, FIPVs have substitutions ofnon-polar, aliphatic or aromatic residues in the protease recognition sites.These changes likely modulate the proteolytic activation of the virus and itsability to productively infect macrophages in vivo.

Feline coronaviruses associated with feline infectious peritonitis have modifications to spike protein activation sites at two discrete positions