title: Role of surface proteins in the deposition kinetics of Cryptosporidium parvum oocysts.
abstract: A radial stagnation point flow system was used to investigate the influence of Cryptosporidium parvum surface properties on oocyst deposition kinetics onto solid surfaces. To determine the role of oocyst surface proteins in adhesion, the deposition kinetics of viable oocysts were compared with the deposition kinetics of oocysts treated (inactivated) with either heat or formalin. Results showed a significantly higher deposition rate with formalin and heat-treated oocysts compared to viable oocysts under identical solution ionic strengths. Low deposition rates and corresponding attachment efficiencies were observed with viable oocysts over the entire range of solution conditions investigated, even at high ionic strengths where DLVO theory predicts the absence of an electrostatic energy barrier. An "electrosteric" repulsion between the viable Cryptosporidium oocyst and the quartz substrate, attributed to proteins on the oocyst surface, is surmised to cause this low deposition rate. Inactivation of the oocysts with either formalin or heat resulted in increased attachment efficiencies over the entire range of ionic strengths examined. It is hypothesized that formalin and heat treatments alter the structure of surface proteins and thus reduce steric repulsion. Formalin treatment was also found to impart an increased hydrophobicity to the oocyst surface and thus greater enhancement in oocyst deposition kinetics compared to heat treatment.
authors.affiliation: Department of Chemical Engineering, Environmental Engineering Program, Yale University, PO Box 208286, New Haven, Connecticut 06520-8286, USA.
authors.forename: Zachary A
authors.initials: ZA
authors.lastname: Kuznar
authors.forename: Menachem
authors.initials: M
authors.lastname: Elimelech
mesh_terms: D000818:Animals; D016785:Cryptosporidium parvum / Q000502:physiology*; D057927:Hydrophobic and Hydrophilic Interactions; D007700:Kinetics; D008565:Membrane Proteins / Q000502:physiology*; D033661:Oocysts / Q000254:growth & development / Q000502:physiology*; D013499:Surface Properties
chemical_list: D008565:Membrane Proteins