PMID- 15562596
OWN - NLM
STAT- MEDLINE
DCOM- 20041209
LR  - 20181113
IS  - 0022-3395 (Print)
IS  - 0022-3395 (Linking)
VI  - 90
IP  - 5
DP  - 2004 Oct
TI  - Microbial adhesion of Cryptosporidium parvum sporozoites: purification of an 
      inhibitory lipid from bovine mucosa.
PG  - 980-90
AB  - Cryptosporidium parvum is a protozoan pathogen of humans and livestock worldwide. 
      Its ability to infect a wide range of species raises questions as to the 
      involvement of a specific host cell receptor for parasite-host recognition. To 
      investigate the mechanism of parasite-host cell recognition, we have developed an 
      in vitro cell suspension binding assay to investigate adhesion of C. parvum 
      sporozoites to host cells. Morphologic features of binding events observed with 
      this assay were identical to those described in natural infections. 
      Glycoconjugates, Madin Darby bovine kidney (MDBK) cell fractions, and plasma 
      membrane vesicles (PMVs) were screened for their ability to block binding of 
      sporozoites to MDBK cells. Mucins, MDBK cell fractions, and PMVs exhibited 
      dose-dependent inhibition of sporozoite binding. The major inhibitory fraction 
      from MDBK cells was found to be insoluble in aqueous medium, nonsaponifiable, and 
      lacking carbohydrate moieties, nitrogen, and phosphorus. Its inhibitory effect 
      was resistant to heat, protease digestion, and glycosidase treatment, suggesting 
      that the inhibitory activity is a lipid or a lipid-like component. The inhibitory 
      activity was purified from MDBK cells, and in larger amounts from bovine small 
      intestinal mucosa, by organic solvent extraction, semipreparative high-pressure 
      liquid chromatography, and preparative high-performance thin-layer 
      chromatography. Biochemical analyses, thin-layer chromatography staining 
      techniques, mass spectrometry, and elemental analysis were used to partially 
      characterize the purified lipid. These results indicate that a host intestinal 
      lipid(s) or a lipid-like component(s) may play an important role in the early 
      stages of host cell invasion by C. parvum.
FAU - Johnson, Julie K
AU  - Johnson JK
AD  - Department of Pathobiology, College of Veterinary Medicine, University of 
      Illinois at Urbana-Champaign, Urbana, Illinois 61802, USA.
FAU - Schmidt, Joann
AU  - Schmidt J
FAU - Gelberg, Howard B
AU  - Gelberg HB
FAU - Kuhlenschmidt, Mark S
AU  - Kuhlenschmidt MS
LA  - eng
GR  - R21 AI044967-01A1/AI/NIAID NIH HHS/United States
GR  - AI44967-01A1/AI/NIAID NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Parasitol
JT  - The Journal of parasitology
JID - 7803124
RN  - 0 (Glycoconjugates)
RN  - 0 (Lipids)
RN  - 0 (Mucins)
SB  - IM
MH  - Animals
MH  - Binding, Competitive
MH  - Cattle
MH  - Cell Adhesion/drug effects
MH  - Cell Line
MH  - Chromatography, High Pressure Liquid
MH  - Cryptosporidiosis/prevention & control
MH  - Cryptosporidium parvum/drug effects/*metabolism
MH  - Glycoconjugates/pharmacology
MH  - Intestinal Mucosa/chemistry/metabolism/*parasitology
MH  - Lipids/isolation & purification/*pharmacology
MH  - Male
MH  - Microscopy, Electron
MH  - Microscopy, Phase-Contrast
MH  - Mucins/pharmacology
PMC - PMC2579925
MID - NIHMS72249
EDAT- 2004/11/26 09:00
MHDA- 2004/12/16 09:00
PMCR- 2008/11/05
CRDT- 2004/11/26 09:00
PHST- 2004/11/26 09:00 [pubmed]
PHST- 2004/12/16 09:00 [medline]
PHST- 2004/11/26 09:00 [entrez]
PHST- 2008/11/05 00:00 [pmc-release]
AID - 10.1645/GE-231R [doi]
PST - ppublish
SO  - J Parasitol. 2004 Oct;90(5):980-90. doi: 10.1645/GE-231R.