. Author manuscript; available in PMC: 2010 Jul 1.

Published in final edited form as: J Microbiol Methods. 2009 May 7;78(1):71–78. doi: 10.1016/j.mimet.2009.05.002

Table 1.

Panel of Als N-terminal protein fragments used for raising and validating anti-Als MAbs

	Gene Sequence^a				Protein Sequence^b

Als Protein	GenBank Accession No.	Sequence Coordinates	No. Codon Corrections	Codon Positions	Amino Acids in Final Protein	Endo H Treated?
Als1	XM712984	1 – 987	1	907	18 – 329	No
Als2	AF024582	1 – 984	1	841	18 – 328	Yes
Als3	U87956	1 – 987	0	--	18 – 329	No
Als4	AF024586	1 – 987	2	739, 937	18 – 329	No
Als5	AF025429	327 – 1313	0	--	18 – 329	No
Als6	AF075293	1 – 996	0	--	19 – 332	Yes
Als7	AY296650	1 – 996	2	34, 634	19 – 332	No
Als9-1	AY269423	1 – 984	1	604	18 – 328	Yes
Als9-2	AY269422	1 – 984	0	--	18 – 328	Yes

The GenBank accession number corresponds to the gene sequence used in the construct. The coordinates of the cloned fragment are shown. CTG codons were changed to TCT using site-directed mutagenesis so that a native C. albicans amino acid sequence would be produced in P. pastoris. The number of codons that were changed is specified, as well as their position within the cloned sequence.

Proteins produced in P. pastoris used the native C. albicans secretory signal sequence, which was cleaved upon export, resulting in the mature protein with the amino acid coordinates shown. N-linked glycosylation was present on four of the Als N-terminal proteins and was removed using Endoglycosidase H as indicated.