Seeding-induced self-assembling protein nanowires dramatically increase the sensitivity of immunoassays.
Aiming to build a supersensitive and easily operable immunoassay, bifunctional protein nanowires were generated by seeding-induced self-assembling of the yeast amyloid protein Sup35p that genetically fused with protein G and an enzyme (methyl-parathion hydrolase, MPH), respectively. The protein nanowires possessed a high ratio of enzyme molecules to protein G, allowing a dramatic increase of the enzymatic signal when protein G was bound to an antibody target. As a result, a 100-fold enhancement of the sensitivity was obtained when applied in the detection of the Yersinia pestis F1 antigen.
Men
Dong
D
State Key Laboratory of Virology, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan 430071, China.
Guo
Yong-Chao
YC
Zhang
Zhi-Ping
ZP
Wei
Hong-ping
HP
Zhou
Ya-Feng
YF
Cui
Zong-Qiang
ZQ
Liang
Xiao-Sheng
XS
Li
Ke
K
Leng
Yan
Y
You
Xiang-Yu
XY
Zhang
Xian-En
XE
D001426:Bacterial Proteins / Q000032:analysis; D004797:Enzyme-Linked Immunosorbent Assay; D053770:Nanowires / Q000737:chemistry*; D009419:Nerve Tissue Proteins / Q000737:chemistry / Q000235:genetics; D010454:Peptide Termination Factors / Q000737:chemistry / Q000235:genetics; D010744:Phosphoric Monoester Hydrolases / Q000737:chemistry / Q000235:genetics; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000235:genetics; D012680:Sensitivity and Specificity
D001426:Bacterial Proteins; C029152:G-substrate; D009419:Nerve Tissue Proteins; D010454:Peptide Termination Factors; D011994:Recombinant Proteins; C068068:SUP35 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; C086725:caf1 protein, Yersinia pestis; D010744:Phosphoric Monoester Hydrolases