Identification and localization of the structural proteins of anguillid herpesvirus 1

Table 2 Envelope proteins of AngHV-1 as identified by 1D gel/nanoLC-MS/MS in the envelope fraction

ORF^a	NCBI ID	Description^b	Predicted molecular mass (kDa)	Number of peptides^c	Mascot score	CyHV-3^d	Membrane protein type	Trans-membrane domain(s)^e	Signal anchor or peptide	N-glyco^f	O-glyco^g
8	282174045		21.2	46	2390		Type 1	o1i	-	4	-
49^h	282174086		26.4	-	-	ORF83	Type 3	i4i	Signal peptide	-	-
51	282174088	Major envelope protein	26.5	137	5970	ORF81	Type 3	i4i	Signal anchor	1	1
66	282174103		42.7	1	46		Type 1	o1i	Signal peptide	4	2
67	282174104	WBV spike protein/Major glycoprotein	152.9	54	2251	ORF99	Type 1	o1i	Signal peptide	13	8
71	282174108		11.4	29	1638		Type 1	o1i	Signal anchor	-	2
78	282174115		16.9	8	609		Type 3	i2i	Signal peptide	-	-
95	282174132	ISAV HA	41.6	190	11573		Type 1	o1i	Signal peptide	5	1
108	282174145	ORF80 family	108.2	4	183		Type 1	o1i	-	3	56
115	282174152		12.1	6	406		Type 1	o1i	Signal anchor	2	-
125	282174162	ORF109 family	120.5	2	189		Type 1	o1i	Signal peptide	16	16

^athe ORF are ordered by number, ^bproperties newly suggested in this paper are presented in italics, ^cnumber of peptides and Mascot score in the envelope fraction, ^dhomologous ORF in CyHV-3 are given, in case of marginal sequence identity (E-value > 10^-5 in a BLAST search limited to members of the Alloherpesviridae family) presented in italics, ^etransmembrane domain(s) and orientation: o = outside, i = inside, number refers to number of transmembrane domains, ^fpredicted N-glycosylation site(s), ^gpredicted O-glycosylation site(s), and ^hAngHV-1 ORF49 was only detected in very low abundance in complete virion preparations, and not in the envelope fraction.

ISSN: 1297-9716