TABLE 2.
Cleavage products | Amino acid at cleavage site position:
|
Reference(s) | ||||||||
---|---|---|---|---|---|---|---|---|---|---|
P6 | P5 | P4 | P3 | P2 | P1 | P1′ | P2′ | |||
Cleaved by PLP1 | ↓
|
|||||||||
MHV p28/p65 | L | K/Ra | G | Y | Ra | Ga | V | K | 12, 20 | |
MHV p65/p210 | W | Ra | F | P | C | Aa | Ga | K | 7 | |
HCoV p9/p87 | G | Ka | R | G | G | Ga | N | V | 17 | |
Cleaved by PLP1 and PLP2 | ||||||||||
HCoV p87/p210b | F | T | K | A | A | G | G | K | 43 | |
Cleaved by PLP2 | ||||||||||
IBV p87/p195c | V | V | C | K | A | Ga | G | K | 25 | |
IBV p195/p41c | V | E | K | K | Aa | Ga | G | I | 26 | |
MHV p210/p44 | Fa | S | L | K | Ga | Ga | A | V | This paper |
A critical determinant for PLP processing as determined by mutagenesis studies.
In vitro transcription-translation studies indicate that both PLP1 and PLP2 can cleave at this site. Critical determinants have not been identified.
A revised alignment study indicates that the domain previously referred to as IBV PLPD has an inactive PLP1 domain and an active PLP2 domain (43).
The arrow indicates where the polyprotein is cleaved.