Detection of disease‐specific PrP in the distal ileum of cattle exposed orally to the agent of bovine spongiform encephalopathy

Terry, Linda A.; Marsh, Sarah; Ryder, Stephen; Hawkins, S. A. C.; Wells, G. A. H.; Spencer, Y. I.

doi:10.1136/vr.152.13.387

Cited by 132 publications

(144 citation statements)

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“…The Peyer's patches in the distal ileum of the cattle were one of the most possible sites on PrP Sc neuroinvasion [30]. As the Peyer's patches are localized in the antimesenteric wall of the ileum, HRP was injected into the intestinal wall in the antimesenteric side of the distal ileum.…”

Section: Discussionmentioning

confidence: 99%

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Localization of Sympathetic, Parasympathetic and Sensory Neurons Innervating the Distal Ileum of the Cattle

Ohmori

Atoji

Saito

et al. 2008

The Journal of Veterinary Medical Science

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ABSTRACT. After oral challenge of the pathological prion protein, the causative agent of bovine spongiform encephalopathy, the pathogen was first detected in the distal ileum and then deposited in the brain. The present study aims determining the possible neuronal transporting pathways from the ileum to the brain in the cattle using a tracer protein. After horseradish peroxidase was injected into the wall of the distal ileum in the calf, almost all labeled neurons were detected in the celiac and cranial mesenteric ganglion complex. Only a few labeled neurons existed in the caudal mesenteric ganglion and the paravertebral ganglia. They were sympathetic postganglionic neurons. In the dorsal root ganglia T5 to L4, some sensory neurons were found to be labeled. Only a small number of parasympathetic preganglionic neurons were labeled in the dorsal motor nucleus of the vagus nerve. No labeled sensory neurons were found in the nodose ganglion. These results suggest that the pathological prion protein is mainly transported to the spinal cord and brain via the sympathetic nervous system and partially via the sensory neurons in the dorsal root ganglia. The vagus nerve does not seem to contribute to the transport of the pathogen from the ileum directly. KEY WORDS: autonomic nervous system, cattle, extrinsic innervation, ileum, retrograde labeling.

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Section: Discussionmentioning

confidence: 99%

“…The distal ileum is one of the most possible sites on prion neuroinvasion, because it is an early detection site of PrP Sc accumulation following the oral prion challenge in the cattle [30]. Via sympathetic, parasympathetic and sensory nerves, PrP Sc may be transported from the ileum to the spinal cord and brain.…”

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confidence: 99%

Localization of Sympathetic, Parasympathetic and Sensory Neurons Innervating the Distal Ileum of the Cattle

Ohmori

Atoji

Saito

et al. 2008

The Journal of Veterinary Medical Science

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“…The infectivity levels in lymphoid tissues greatly vary depending on the prion agent or strain type [12]. Some scrapie strains, the CWD and vCJD agents are able to replicate in such tissues [2,178,200] whereas accumulation of BSE prions in cattle is only evidenced in the terminal ileum, in experimental infection yet not in natural cases [191]. Intriguingly, a prion agent can become lymphotropic upon interspecies transmission, as seen for BSE in sheep [75] or vCJD in humans [200].…”

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confidence: 99%

Prion agent diversity and species barrier

2008

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-Mammalian prions are the infectious agents responsible for transmissible spongiform encephalopathies (TSE), a group of fatal, neurodegenerative diseases, affecting both domestic animals and humans. The most widely accepted view to date is that these agents lack a nucleic acid genome and consist primarily of PrP Sc , a misfolded, aggregated form of the host-encoded cellular prion protein (PrP C ) that propagates by autocatalytic conversion and accumulates mainly in the brain. The BSE epizooty, allied with the emergence of its human counterpart, variant CJD, has focused much attention on two characteristics that prions share with conventional infectious agents. First, the existence of multiple prion strains that impose, after inoculation in the same host, specific and stable phenotypic traits such as incubation period, molecular pattern of PrP Sc and neuropathology. Prion strains are thought to be enciphered within distinct PrP Sc conformers. Second, a transmission barrier exists that restricts the propagation of prions between different species. Here we discuss the possible situations resulting from the confrontation between species barrier and prion strain diversity, the molecular mechanisms involved and the potential of interspecies transmission of animal prions, including recently discovered forms of TSE in ruminants.prion / strain / misfolding / species barrier / PrP Table of Mammalian prion diseases or transmissible spongiform encephalopathies (TSE) form a group of related, invariably fatal neurodegenerative disorders of both animals and humans. The brain pathology consists of spongiosis, astrocytosis, neuronal loss and neural tissue from affected individuals contains an infectious agent, the prion, setting these diseases apart from other neurodegenerative diseases. Prion replication is thought to involve in essence the self-perpetuating conversion of the host-encoded cellular prion protein (PrP C ) into a misfolded form (PrP Sc ) that tends to aggregate and may be neurotoxic (for reviews [1,157]). Prion replication may also occur in lymphoid tissues but is there poorly if not pathogenic (for review [126], [133]). PrP C is a protein with two variably occupied glycosylation sites. It is attached at the outer of the plasma membrane by a glycosylphosphatidylinositol anchor. Its secondary structure is rich in alpha-helix and the protein is likely to be in a monomeric state in mild detergents. While its precise physiological function has not been assigned, PrP C is essential for prion replication and neurotoxicity to occur [57,129]. Upon infection, PrP C is refolded -without apparent post-translational modification -into beta-sheet -rich PrP Sc , initially in the presence of exogenous PrP Sc and then by an autocatalytic process. It leads to the formation of aggregates, sometimes of amyloid type, that can be differentiated from PrP C because of their partial resistance to protease digestion and of their insolubility into non-denaturing detergents [153]. Proteinase K, the most commonly used protease, di...

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“…PrP sc accumulates mainly in the specified-risk material, such as brain, spinal cord and dorsal root ganglion, and it has been suggested that PrP sc may be transmitted from distal ileum or tonsil to peripheral nervous system and then invade into central nervous system. However, PrP sc deposition has been also reported in peripheral tissues of BSE cattle [2][3][4][5] . In the 94-month-old cow infected with PrP sc , protease A-resistant prion protein was found in peripheral nervous system such as ischiadic nerve and in adrenal gland 6) .…”

Section: Introductionmentioning

confidence: 99%

Ratio of Peripheral Nervous Tissues in Tongues, Skeletal Muscles and Intestines in Cows

Zhu

Matoba

Hara

et al. 2008

Okajimas Folia Anat. Jpn.

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Detection of disease‐specific PrP in the distal ileum of cattle exposed orally to the agent of bovine spongiform encephalopathy

Cited by 132 publications

References 33 publications

Localization of Sympathetic, Parasympathetic and Sensory Neurons Innervating the Distal Ileum of the Cattle

Localization of Sympathetic, Parasympathetic and Sensory Neurons Innervating the Distal Ileum of the Cattle

Prion agent diversity and species barrier

Ratio of Peripheral Nervous Tissues in Tongues, Skeletal Muscles and Intestines in Cows

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