scholarly journals Peer Review #2 of "Leishmania amazonensis promastigotes in 3D Collagen I culture: an in vitro physiological environment for the study of extracellular matrix and host cell interactions (v0.2)"

2014 ◽  
Keyword(s):  
Extracellular Matrix ◽  
Host Cell ◽  
Peer Review ◽  
Cell Interactions ◽  
Leishmania Amazonensis ◽  
Collagen I ◽  
Host Cell Interactions ◽  
3D Collagen

scholarly journals Leishmania amazonensispromastigotes in 3D Collagen I culture: anin vitrophysiological environment for the study of extracellular matrix and host cell interactions

PeerJ ◽  
2014 ◽  
Vol 2 ◽  
pp. e317 ◽  
Author(s):  
Debora B. Petropolis ◽  
Juliany C.F. Rodrigues ◽  
Nathan B. Viana ◽  
Bruno Pontes ◽  
Camila F.A. Pereira ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Host Cell ◽  
Cell Interactions ◽  
Collagen I ◽  
Host Cell Interactions ◽  
3D Collagen

scholarly journals Identification and Characterization of Cryptosporidium parvum Clec, a Novel C-Type Lectin Domain-Containing Mucin-Like Glycoprotein

2013 ◽  
Vol 81 (9) ◽  
pp. 3356-3365 ◽  
Author(s):  
Seema Bhalchandra ◽  
Jacob Ludington ◽  
Isabelle Coppens ◽  
Honorine D. Ward
Keyword(s):  
Host Cell ◽  
Transmembrane Domain ◽  
Cell Interactions ◽  
Apical Region ◽  
Content Type ◽  
Lectin Domain ◽  
Loop Region ◽  
Wide Range ◽  
Host Cell Interactions

ABSTRACTCryptosporidiumspecies are waterborne apicomplexan parasites that cause diarrheal disease worldwide. Although the mechanisms underlyingCryptosporidium-host cell interactions are not well understood, mucin-like glycoproteins of the parasite are known to mediate attachment and invasionin vitro. We identifiedC. parvumClec (CpClec), a novel mucin-like glycoprotein that contains a C-type lectin domain (CTLD) and has orthologs inC. hominisandC. muris. CTLD-containing proteins are ligand-binding proteins that function in adhesion and signaling and are present in a wide range of organisms, from humans to viruses. However, this is the first report of a CTLD-containing protein in protozoa and inApicomplexa. CpClec is predicted to be a type 1 membrane protein, with a CTLD, an O-glycosylated mucin-like domain, a transmembrane domain, and a cytoplasmic tail containing a YXXϕ sorting motif. The predicted structure ofCpClec displays several characteristics of canonical CTLD-containing proteins, including a long loop region hydrophobic core associated with calcium-dependent glycan binding as well as predicted calcium- and glycan-binding sites.CpClec expression duringC. parvuminfectionin vitrois maximal at 48 h postinfection, suggesting that it is developmentally regulated. The 120-kDa mass of nativeCpClec is greater than predicted, most likely due to O-glycosylation.CpClec is localized to the surface of the apical region and to dense granules of sporozoites and merozoites. Taken together, these findings, along with the known functions ofC. parvummucin-like glycoproteins and of CTLD-containing proteins, strongly implicate a significant role forCpClec inCryptosporidium-host cell interactions.

Fluorescent Eimeria bovis sporozoites and meront stages in vitro: a helpful tool to study parasite–host cell interactions

2008 ◽  
Vol 102 (4) ◽  
pp. 777-786 ◽  
Author(s):  
Carlos Hermosilla ◽  
Ivonne Stamm ◽  
Anja Taubert ◽  
Kathleen Lutz ◽  
Horst Zahner ◽  
...  
Keyword(s):  
Host Cell ◽  
Cell Interactions ◽  
Helpful Tool ◽  
Host Cell Interactions ◽  
Eimeria Bovis
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