Dataset Information

Identification and validation of protective glycoproteins in Haemonchus contortus H11

ABSTRACT: 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 been shown to induce high levels (72-95%) of protection, but single or two recombinant molecules of H11 are consistently unsuccessful. An increasing number of aminopeptidases related to H11 have been characterized in the past three decades, but little is known about which ones are the key contributors to protective immunity. Our recent work has revealed that the immunoprotective effect of H11 is primarily associated with its N-glycan moieties. To identify key immunoprotective glycoproteins derived from H11 antigen, we employed glycan-related protective IgG antibodies combined with LC-MS/MS analysis and identified five glycosylated H11 proteins: H11, H11-1, H11-2, H11-4, and H11-5. Subsequently, we utilized the baculovirus-insect cell expression system and successfully expressed four H11 recombinant proteins including rH11, rH11-1, rH11-2 and rH11-4, which demonstrated similar aminopeptidase activity and comparable high-mannose and di-fucosylated N-glycan structures to those found on native H11. Immunisation of goats with a cocktail of four rH11s induced a 66.29% reduction (p > 0.05) in total worm burden and cumulative faecal egg counts. High level of anti-rH11s IgG which could inhibit H. contortus intestinal aminopeptidase activity and larval development. Collectively, our study identified glycoprotein antigens from H11 and assessed their protective efficacy of a recombinant cocktail expressed in insect cells. This work will provide valuable insights into further development of recombinant vaccines against parasitic nematodes.

INSTRUMENT(S):

ORGANISM(S): Haemonchus Contortus (barber Pole Worm)

TISSUE(S): Cell Suspension Culture

SUBMITTER: Hui Liu

LAB HEAD: Chunqun Wang

PROVIDER: PXD060969 | Pride | 2025-05-07

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	Glycans_data_released_from_PNGase_A_and_analysed_by_Data_Explorer_Software.zip	Other
	Glycans_data_released_from_PNGase_F_and_analysed_by_Data_Explorer_Software.zip	Other
	Glycans_released_from_recombinant_H11_proteins_by_PNGase_F_and_PNGase_A_MSMS.zip	Other

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Identification and validation of protective glycoproteins in <i>Haemonchus contortus</i> H11.

Liu Hui H Zhang Yao Y Li Jiarui J Liu Feng F Ye Lisha L Liu Xin X Wang Chunqun C Hu Min M

Frontiers in immunology 20250228

Barbervax is the first and only available vaccine to protect animals against <i>Haemonchus contortus</i> - 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 been shown to induce high levels (72-95%) of protection, but single or two recombinant molecules of H11 are consistently unsuccessful. An increasing number of aminopeptidases related to H11 have ...[more]

PMID: 40093001

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Project description:Alterations in glycosylation are seen in many types of cancer, including colorectal cancer (CRC). CRC is known to display glycosylation alterations. Glycans, the sugar moieties of glycoconjugates, are involved in many important functions relevant to cancer, such as cell signaling and adhesion, and may can be of value as biomarkers. In this study, we have used mass spectrometry to analyze the N-glycan profiles of 35 CRC tissue samples from patients with tumors in the right or left colon and 10 healthy tissue samples from non-CRC patients who underwent operations for other reasons. The tumor samples were divided into groups depending on tumor location (right or left colon) and stage (II or III), while the healthy samples were divided into right or left side of the colon. The levels of neutral and acidic N-glycan compositions and glycan classes were analyzed in a total of ten different groups. Surprisingly, there were no significant differences in glycan levels when all right- and left-sided CRC samples were compared, and few differences (such as in the abundance of the neutral N-glycan H3N5) were seen when the samples were divided according to both location and stage. Multiple significant differences were found in the levels of glycans and glycan classes when stage II and III samples were compared, and these glycans could be of value as candidates for new markers of cancer progression. In order to validate our findings, we analyzed healthy tissue samples from the right and left colon and found no significant differences in the levels of any of the glycans analyzed, confirming that our findings when comparing CRC samples from the right and left colon are not due to normal variations in the levels of glycans between the healthy right and left colon. Additionally, the levels of the acidic glycans H4N3F1P1, H5N4F1P1, and S1H5N4F1 were found to change in a cancer-specific but colon location-nonspecific manner, indicating that CRC affects glycan levels in similar ways, regardless of tumor location.

Dataset Information

Identification and validation of protective glycoproteins in Haemonchus contortus H11

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Publications

Identification and validation of protective glycoproteins in <i>Haemonchus contortus</i> H11.

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Dataset Information

Identification and validation of protective glycoproteins in Haemonchus contortus H11

Dataset's files

Publications

Identification and validation of protective glycoproteins in &lt;i&gt;Haemonchus contortus&lt;/i&gt; H11.

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OmicsDI is part of the ELIXIR infrastructure

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Identification and validation of protective glycoproteins in <i>Haemonchus contortus</i> H11.