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.

scholarly journals Role of Retrograde Trafficking in Stress Response, Host Cell Interactions, and Virulence of Candida albicans

2013 ◽  
Vol 13 (2) ◽  
pp. 279-287 ◽  
Author(s):  
Yaoping Liu ◽  
Norma V. Solis ◽  
Clemens J. Heilmann ◽  
Quynh T. Phan ◽  
Aaron P. Mitchell ◽  
...  
Keyword(s):  
Candida Albicans ◽  
Host Cell ◽  
Signaling Pathway ◽  
Stress Resistance ◽  
Cell Interactions ◽  
Content Type ◽  
Retrograde Trafficking ◽  
Host Cell Interactions ◽  
Vacuolar Protein ◽  
Calcineurin Signaling

ABSTRACTInSaccharomyces cerevisiae, the vacuolar protein sorting complexes Vps51/52/53/54 and Vps15/30/34/38 are essential for efficient endosome-to-Golgi complex retrograde transport. Here we investigated the function of Vps15 and Vps51, representative members of these complexes, in the stress resistance, host cell interactions, and virulence ofCandida albicans. We found thatC. albicansvps15Δ/Δ andvps51Δ/Δ mutants had abnormal vacuolar morphology, impaired retrograde protein trafficking, and dramatically increased susceptibility to a variety of stressors. These mutants also had reduced capacity to invade and damage oral epithelial cellsin vitroand attenuated virulence in the mouse model of oropharyngeal candidiasis. Proteomic analysis of the cell wall of thevps51Δ/Δ mutant revealed increased levels of the Crh11 and Utr2 transglycosylases, which are targets of the calcineurin signaling pathway. The transcript levels of the calcineurin pathway membersCHR11,UTR2,CRZ1,CNA1, andCNA2were elevated in thevps15Δ/Δ andvps51Δ/Δ mutants. Furthermore, these strains were highly sensitive to the calcineurin-specific inhibitor FK506. Also, deletion ofCHR11andUTR2further increased the stress susceptibility of these mutants. In contrast, overexpression ofCRH11andUTR2partially rescued their defects in stress resistance, but not host cell interactions. Therefore, intact retrograde trafficking inC. albicansis essential for stress resistance, host cell interactions, and virulence. Aberrant retrograde trafficking stimulates the calcineurin signaling pathway, leading to the increased expression of Chr11 and Utr2, which enablesC. albicansto withstand environmental stress.

scholarly journals Molecular Cloning and Expression of a Gene EncodingCryptosporidium parvum Glycoproteins gp40 and gp15

2000 ◽  
Vol 68 (7) ◽  
pp. 4108-4116 ◽  
Author(s):  
Ana Maria Cevallos ◽  
Xiaoping Zhang ◽  
Matthew K. Waldor ◽  
Smitha Jaison ◽  
Xiaoyin Zhou ◽  
...  
Keyword(s):  
Host Cell ◽  
Molecular Mechanisms ◽  
Diarrheal Disease ◽  
Cell Interactions ◽  
Host Cells ◽  
Surface Glycoprotein ◽  
Cloning And Expression ◽  
Apical Region ◽  
Hydrophobic Region ◽  
Host Cell Interactions

ABSTRACT Cryptosporidium parvum is a significant cause of diarrheal disease worldwide. The specific molecules that mediateC. parvum-host cell interactions and the molecular mechanisms involved in the pathogenesis of cryptosporidiosis are unknown. In this study we have shown that gp40, a mucin-like glycoprotein, is localized to the surface and apical region of invasive stages of the parasite and is shed from its surface. gp40-specific antibodies neutralize infection in vitro, and native gp40 binds specifically to host cells, implicating this glycoprotein in C. parvum attachment to and invasion of host cells. We have cloned and sequenced a gene designated Cpgp40/15 that encodes gp40 as well as gp15, an antigenically distinct, surface glycoprotein also implicated in C. parvum-host cell interactions. Analysis of the deduced amino acid sequence of the 981-bp Cpgp40/15revealed the presence of an N-terminal signal peptide, a polyserine domain, multiple predicted O-glycosylation sites, a single potential N-glycosylation site, and a hydrophobic region at the C terminus, a finding consistent with what is required for the addition of a GPI anchor. There is a single copy ofCpgp40/15 in the C. parvum genome, and this gene does not contain introns. Our data indicate that the twoCpgp40/15-encoded proteins, gp40 and gp15, are products of proteolytic cleavage of a 49-kDa precursor protein which is expressed in intracellular stages of the parasite. The surface localization of gp40 and gp15 and their involvement in the host-parasite interaction suggest that either or both of these glycoproteins may serve as effective targets for specific preventive or therapeutic measures for cryptosporidiosis.

scholarly journals Epithelial Interleukin-8 Responses to Oral Bacterial Biofilms

2011 ◽  
Vol 18 (10) ◽  
pp. 1770-1772 ◽  
Author(s):  
R. Peyyala ◽  
S. Kirakodu ◽  
K. F. Novak ◽  
J. L. Ebersole
Keyword(s):  
Host Cell ◽  
Contact Lenses ◽  
Bacterial Biofilms ◽  
Content Type ◽  
Oral Epithelial Cells ◽  
Cell Responses ◽  
Host Cell Interactions ◽  
Oral Epithelial ◽  
Novel Model

ABSTRACTAnin vitromodel of bacterial biofilms on rigid gas-permeable contact lenses (RGPLs) was developed to challenge oral epithelial cells. This novel model provided seminal data on oral biofilm-host cell interactions, and with selected bacteria, the biofilms were more effective than their planktonic counterparts at stimulating host cell responses.

scholarly journals Pivotal Roles for Ribonucleases in Streptococcus pneumoniae Pathogenesis

mBio ◽  
2021 ◽  
Author(s):  
Dhriti Sinha ◽  
Jacob P. Frick ◽  
Kristen Clemons ◽  
Malcolm E. Winkler ◽  
Nicholas R. De Lay
Keyword(s):  
Gene Expression ◽  
Streptococcus Pneumoniae ◽  
Host Cell ◽  
Cell Interactions ◽  
Human Pathogen ◽  
Protein Coding ◽  
Content Type ◽  
Key Players ◽  
Host Cell Interactions ◽  
Host Tissues

Streptococcus pneumoniae is a notorious human pathogen that adapts to conditions in distinct host tissues and responds to host cell interactions by adjusting gene expression. RNases are key players that modulate gene expression by mediating the turnover of regulatory and protein-coding transcripts.

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
Sign in / Sign up

Export Citation Format

Share Document