Skip to Main Content
DownloadHi-Res Photo

Shuaiqi Guo, PhD

Associate Research Scientist

Contact Information

Shuaiqi Guo, PhD
Liu Lab

Research Summary

The emergence of antibiotic-resistant bacteria poses a substantial health threat to humans. As conventional antibiotics are losing their potency, alternative solutions are urgently needed to combat bacterial infections. Bacteria use complex membrane-embedded protein assemblies called nanomachines to acquire nutrients, adhere to various surfaces and cells, and expel toxins from and inject effectors into host cells. Thus, these nanomachines are essential for bacterial virulence and survival, enabling infection and colonization of specific niches. In the Liu Lab, I use cryo-electron tomography to investigate the in situ structural biology of bacterial nanomachines involved in protein secretion and adhesion. Combined with knowledge acquired from biochemical and genetic studies, we aim to reveal key mechanistic insights needed to impair virulence by disrupting the functions of these nanomachines, a promising alternative route to treat bacterial infections without provoking resistance.

Coauthors

Research Interests

Drug Resistance, Microbial; Molecular Biology; Molecular Structure; Cryoelectron Microscopy

Selected Publications

  • FliL ring enhances the function of periplasmic flagella.Guo S, Xu H, Chang Y, Motaleb MA, Liu J. FliL ring enhances the function of periplasmic flagella. Proceedings Of The National Academy Of Sciences Of The United States Of America 2022, 119: e2117245119. PMID: 35254893, PMCID: PMC8931381, DOI: 10.1073/pnas.2117245119.
  • Structural Basis of Ligand Selectivity by a Bacterial Adhesin Lectin Involved in Multispecies Biofilm Formation.Guo S, Vance TDR, Zahiri H, Eves R, Stevens C, Hehemann JH, Vidal-Melgosa S, Davies PL. Structural Basis of Ligand Selectivity by a Bacterial Adhesin Lectin Involved in Multispecies Biofilm Formation. MBio 2021, 12 PMID: 33824212, PMCID: PMC8092209, DOI: 10.1128/mBio.00130-21.
  • Role of the major determinant of polar flagellation FlhG in the endoflagella-containing spirochete Leptospira.Fule L, Halifa R, Fontana C, Sismeiro O, Legendre R, Varet H, Coppée JY, Murray GL, Adler B, Hendrixson DR, Buschiazzo A, Guo S, Liu J, Picardeau M. Role of the major determinant of polar flagellation FlhG in the endoflagella-containing spirochete Leptospira. Molecular Microbiology 2021, 116: 1392-1406. PMID: 34657338, DOI: 10.1111/mmi.14831.
  • Molecular basis for inhibition of adhesin-mediated bacterial-host interactions through a peptide-binding domain.Guo S, Zahiri H, Stevens C, Spaanderman DC, Milroy LG, Ottmann C, Brunsveld L, Voets IK, Davies PL. Molecular basis for inhibition of adhesin-mediated bacterial-host interactions through a peptide-binding domain. Cell Reports 2021, 37: 110002. PMID: 34788627, DOI: 10.1016/j.celrep.2021.110002.
  • Enhancing the Freeze-Thaw Durability of Concrete through Ice Recrystallization Inhibition by Poly(vinyl alcohol).Qu Z, Guo S, Sproncken CCM, Surís-Valls R, Yu Q, Voets IK. Enhancing the Freeze-Thaw Durability of Concrete through Ice Recrystallization Inhibition by Poly(vinyl alcohol). ACS Omega 2020, 5: 12825-12831. PMID: 32548466, PMCID: PMC7288587, DOI: 10.1021/acsomega.0c00555.
  • RTX Adhesins are Key Bacterial Surface Megaproteins in the Formation of Biofilms.Guo S, Vance TDR, Stevens CA, Voets I, Davies PL. RTX Adhesins are Key Bacterial Surface Megaproteins in the Formation of Biofilms. Trends In Microbiology 2019, 27: 453-467. PMID: 30658900, DOI: 10.1016/j.tim.2018.12.003.
  • Phasing with calcium at home.Guo S, Campbell R, Davies PL, Allingham JS. Phasing with calcium at home. Acta Crystallographica. Section F, Structural Biology Communications 2019, 75: 377-384. PMID: 31045567, PMCID: PMC6497102, DOI: 10.1107/S2053230X19004151.
  • Structure and functional analysis of a bacterial adhesin sugar-binding domain.Vance TDR, Guo S, Assaie-Ardakany S, Conroy B, Davies PL. Structure and functional analysis of a bacterial adhesin sugar-binding domain. PloS One 2019, 14: e0220045. PMID: 31335890, PMCID: PMC6650083, DOI: 10.1371/journal.pone.0220045.
  • Conserved structural features anchor biofilm-associated RTX-adhesins to the outer membrane of bacteria.Guo S, Langelaan DN, Phippen SW, Smith SP, Voets IK, Davies PL. Conserved structural features anchor biofilm-associated RTX-adhesins to the outer membrane of bacteria. The FEBS Journal 2018, 285: 1812-1826. PMID: 29575515, DOI: 10.1111/febs.14441.
  • Structure of a 1.5-MDa adhesin that binds its Antarctic bacterium to diatoms and ice.Guo S, Stevens CA, Vance TDR, Olijve LLC, Graham LA, Campbell RL, Yazdi SR, Escobedo C, Bar-Dolev M, Yashunsky V, Braslavsky I, Langelaan DN, Smith SP, Allingham JS, Voets IK, Davies PL. Structure of a 1.5-MDa adhesin that binds its Antarctic bacterium to diatoms and ice. Science Advances 2017, 3: e1701440. PMID: 28808685, PMCID: PMC5550230, DOI: 10.1126/sciadv.1701440.
  • Modeling repetitive, non-globular proteins.Basu K, Campbell RL, Guo S, Sun T, Davies PL. Modeling repetitive, non-globular proteins. Protein Science : A Publication Of The Protein Society 2016, 25: 946-58. PMID: 26914323, PMCID: PMC4838656, DOI: 10.1002/pro.2907.
  • Blocking rapid ice crystal growth through nonbasal plane adsorption of antifreeze proteins.Olijve LL, Meister K, DeVries AL, Duman JG, Guo S, Bakker HJ, Voets IK. Blocking rapid ice crystal growth through nonbasal plane adsorption of antifreeze proteins. Proceedings Of The National Academy Of Sciences Of The United States Of America 2016, 113: 3740-5. PMID: 26936953, PMCID: PMC4833260, DOI: 10.1073/pnas.1524109113.
  • Putting life on ice: bacteria that bind to frozen water.Bar Dolev M, Bernheim R, Guo S, Davies PL, Braslavsky I. Putting life on ice: bacteria that bind to frozen water. Journal Of The Royal Society, Interface / The Royal Society 2016, 13 PMID: 27534698, PMCID: PMC5014055, DOI: 10.1098/rsif.2016.0210.
  • Ca2+-stabilized adhesin helps an Antarctic bacterium reach out and bind ice.Vance TD, Olijve LL, Campbell RL, Voets IK, Davies PL, Guo S. Ca2+-stabilized adhesin helps an Antarctic bacterium reach out and bind ice. Bioscience Reports 2014, 34 PMID: 24892750, PMCID: PMC4083281, DOI: 10.1042/BSR20140083.
  • Role of Ca²⁺ in folding the tandem β-sandwich extender domains of a bacterial ice-binding adhesin.Guo S, Garnham CP, Karunan Partha S, Campbell RL, Allingham JS, Davies PL. Role of Ca²⁺ in folding the tandem β-sandwich extender domains of a bacterial ice-binding adhesin. The FEBS Journal 2013, 280: 5919-32. PMID: 24024640, DOI: 10.1111/febs.12518.
  • Re-evaluation of a bacterial antifreeze protein as an adhesin with ice-binding activity.Guo S, Garnham CP, Whitney JC, Graham LA, Davies PL. Re-evaluation of a bacterial antifreeze protein as an adhesin with ice-binding activity. PloS One 2012, 7: e48805. PMID: 23144980, PMCID: PMC3492233, DOI: 10.1371/journal.pone.0048805.
Edit Profile