Identification and Validation of Vaccine Candidate Proteins by 2-Dimensional Mass Spectrometry Analysis of Group A Streptococcus

Identification and Validation of Vaccine Candidate Proteins by 2-Dimensional Mass Spectrometry Analysis of Group A Streptococcus

• Surface proteins of bacteria are involved in the adhesion and
invasion of host cells
• We characterized the surface proteome of group A Streptococcus
using multidimensional protein identification technology.
• The relative abundance of identified proteins was determined using
peak height calculations from ion intensity.
• The surface accessibility of identified proteins is determined by a
comparative analysis of surface digests and total protein digests,
as well as PSORTB, a cell localization prediction algorithm.
• 302 proteins were identified in a surface protein digestion of the
M1 Strain. A total of 311 proteins were identified in a surface protein
digestion of the M3 strain.
• M1 Protein type 1 (SPy2018) was identified in both strains
as the highest abundance protein, a fact known to be true.
• These proteomics results are validated by literature, PSortB,
and biological data.
• Proteins identified by this method include the most protective
antigens in literature.
• We identified 12 proteins of interest for potential vaccine targets.