The TvLEGU-1, a Legumain-Like Cysteine Proteinase, Plays a Key Role in Trichomonas vaginalis Cytoadherence

Table 1

Peptides identified by MALDI-TOF-MS analysis of the three TvLEGU-1 protein spots of Trichomonas vaginalis detected by the anti-TvLEGU-1r antibody.

Peptide number^a	Position^b (aa)	Number in the sequence^c	𝑚/𝑧 (av)^d	Spot 1^e	Spot 2^e	Spot 3^e	Amino acid sequence^f
1	13–27	I	1749.9186	−	+	+	FAVLIAGSNDFYNYR
2	28–41	II	1734.9719	+	+	+	HQADIFNMYQQLVK
3	41–66	III	2774.0025	−	+	+	GFDDQHITMMAYDDIALSSENPFR
4	42–66	IV	2930.1882	−	+	+	RGFDDQHITMMAYDDIALSSENPFR
5	75–84	V	1101.2126	−	+	+	HVNIYPGSSK
6	85–105	VI	2399.6528	−	+	+	INYAHNSVTADQFYTVLTTLK
7	144–151	VII	911.4059	+	+	−	AFDTMEAK
8	157–174	VIII	1994.1426	−	+	+	LFFGIEACYSGSVAAVFR
9	157–176	IX	2193.5226	+	+	+	LFFGIEACYSGSVAAVFRAK
10	232–248	X	1931.1107	−	+	+	AQTTGSHVCYYGDVNMK

^aConsecutive number assigned to the identified peptides. ^bPosition in amino acids (aa) residues of the identified peptides (start-end) in the aa sequence of the T. vaginalis TvLEGU-1 [38]. ^cArbitrary nomenclature used to describe the ten identified peptides in T. vaginalis TvLEGU-1 (see Supplementary Figure  1S in Supplementary Material available online at doi:10.1155/2012/561979). ^dPeptide mass average 𝑚/𝑧 (av) identified by MALDI-TOF-MS after tryptic digestion of the three protein spots obtained from 2DE of protease-rich extracts from T. vaginalis grown in normal iron conditions (Figure 1). ^ePresence (+) or absence (−) of the peptides identified by MALDI-TOF-MS in the three TvLEGU-1 protein spots analyzed. ^fAmino acid sequence of the peptides obtained from a theoretical tryptic digestion of the deduced aa sequence of TvLEGU-1 [38] with identical masses to the experimental one (Supplementary Figure  1S).