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ProteomicsIdentification and validation of protective glycoproteins in Haemonchus contortus H11
Barbervax is the first and only available vaccine to protect animals against Haemonchus contortus - one of the most pathogenic parasites of small ruminants. This vaccine contains a kind of native antigen called H11, a glycoprotein complex derived from integral gut of this parasite. Native H11 has be...
ORGANISM(S): Haemonchus contortus (Barber pole worm) 
2025-05-07 | PXD060969 | Pride
Haemonchus contortus N-glycan H11 Immunoprotection Vaccine Glycoprotein Insect cells Recombinant antigen 
ProteomicsH11-induced immune protection is predominantly linked to N-glycan moieties
Parasitic nematodes of humans, animals and plants cause significant economic losses worldwide. Control of these pathogens is currently challenging due to the widespread problem of nematode anthelmintic resistance. Unfortunately, most efforts to develop anti-nematode vaccines for use in animals and h...
ORGANISM(S): Haemonchus contortus (Barber pole worm) 
2022-10-20 | PXD037140 | Pride
Parasitic nematode N-glycan Immunoprotection Vaccine N-glycosylation H11 antigen Igg antibodies 
ProteomicsSite- and Structure-Specific Characterization of Glycoproteins of H11: Potent Vaccine Candidates against Parasitic Worm Haemonchus
Parasitic worms (helminths) represent a major class of human and animal pathogens that impact agriculture and economies worldwide. Over the past few decades, Mass spectrometry (MS)-based glycomics studies have revealed that helminths possess an abundance of complex and unique glycoconjugates that in...
ORGANISM(S): Haemonchus contortus (Barber pole worm) 
2025-12-17 | PXD068910 | Pride
Parasitic worm  n-glycoproteome  intact n-glycopeptide analysis  vaccine  glycan analysis 
UnknownIdentification and validation of protective glycoproteins in <i>Haemonchus contortus</i> H11.
Not available
S-EPMC11906660 | biostudies-literature
UnknownUse of clustered regularly interspaced short palindromic repeat sequence polymorphisms for specific detection of enterohemorrhagic Escherichia coli strains of serotypes O26:H11, O45:H2, O103:H2, O111:H8, O121:H19, O145:H28, and O157:H7 by real-time PCR.
Not available
S-EPMC3503007 | biostudies-literature
UnknownSequence-based typing of genetic targets encoded outside of the O-antigen gene cluster is indicative of Shiga toxin-producing Escherichia coli serogroup lineages.
Not available
S-EPMC2884935 | biostudies-literature
UnknownAnti-CTLA-4 therapy requires an Fc domain for efficacy.
Not available
S-EPMC5899492 | biostudies-literature
GenomicsEscherichia coli 900105 (10e)
Escherichia coli 900105 (10e) Genome sequencing project
PRJNA51137 | ENA
GenomicsEscherichia coli H30
Escherichia coli H30 Genome sequencing project
PRJNA51093 | ENA
UnknownThe evolutionary divergence of Shiga toxin-producing Escherichia coli is reflected in clustered regularly interspaced short palindromic repeat (CRISPR) spacer composition.
Not available
S-EPMC3754162 | biostudies-literature
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