**5. Conclusions and future outlook**

Prion strains and the interspecies barriers are still enigmatic phenomena. One of the surprising things about prion protein is that this single protein can fold up in

#### **Figure 1.**

*Prion strain emergence and interspecies transmission. The original prion strains were named as Kuru in human, BSE in cows, TSE in goat and sheep, and TME in minks. PMCA and RT-QuiC mobilized the prion strain characterization. The interspecies transmission of prions linked with host PrP oligomerization role, appearance of subassemblies named as quasispecies, tissue tropism, incubation period of prions, symptomatic stages of the diseases, and host range.*

**65**

provided the original work is properly cited.

and ingazerr@med.uni-goettingen.de

*Prion Protein Strain Diversity and Disease Pathology*

in the characterization of the prion strain.

novel therapeutic approaches to such devastating disorders.

function as well as from the DZNE clinical project (Helmholtz).

Saima Zafar1,2\*, Neelam Younas1,2, Mohsin Shafiq1,2 and Inga Zerr1,2\*

Goettingen (UMG), Georg-August University, Goettingen, Germany

\*Address all correspondence to: sz\_awaan@yahoo.com

We have no conflict of interest to declare.

so many different ways that are toxic and cause disease. Recent advances in PrPSc amplification methods, i.e., PMCA and RT-QuIC, might lead to clear improvements

From last many years, prion protein strain characterization and impact on disease are under debate. The use of prion transgenic models has been influential for studying and clarifying the molecular mechanisms in which the protein is involved. The ability to cross species barrier may be a result of either quasispecies theory or host PrP impact on progressive templating deformation upon oligomerization theory (**Figure 1**). These phenomena are mostly time dependent. By learning the structural variation and potential interspecies transmissions, we may progress toward the understanding of disease pathology and subsequently development of

The study was performed within the recently established Clinical Dementia Center at the University Medical Hospital Goettingen and was partly supported by grants from the EU Joint Program Neurodegenerative Disease Research (JPND ± DEMTEST) (Biomarker-based diagnosis of rapid progressive dementias-optimization of diagnostic protocols, 01ED1201A). This work was supported by a grant from Helmholtz-Alberta Initiative-Infectious Diseases Research (HAI-IDR) and APRI-Human prions distinguishing sporadic from familial forms via structure and

*DOI: 10.5772/intechopen.80702*

**Acknowledgements**

**Conflict of interest**

**Author details**

© 2019 The Author(s). Licensee IntechOpen. This chapter is distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/ by/3.0), which permits unrestricted use, distribution, and reproduction in any medium,

1 Department of Neurology, Clinical Dementia Center, University Medical Center

2 German Center for Neurodegenerative Diseases (DZNE), Goettingen, Germany

*Prion Protein Strain Diversity and Disease Pathology DOI: 10.5772/intechopen.80702*

so many different ways that are toxic and cause disease. Recent advances in PrPSc amplification methods, i.e., PMCA and RT-QuIC, might lead to clear improvements in the characterization of the prion strain.

From last many years, prion protein strain characterization and impact on disease are under debate. The use of prion transgenic models has been influential for studying and clarifying the molecular mechanisms in which the protein is involved. The ability to cross species barrier may be a result of either quasispecies theory or host PrP impact on progressive templating deformation upon oligomerization theory (**Figure 1**). These phenomena are mostly time dependent. By learning the structural variation and potential interspecies transmissions, we may progress toward the understanding of disease pathology and subsequently development of novel therapeutic approaches to such devastating disorders.
