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Volume 5, Issue 3(Suppl) Biochem Anal Biochem 2016
ISSN: 2161-1009, Biochem an open access journal
Page 58
Biochemistry 2016
October 10-12, 2016
conferenceseries.com
Biochemistry
October 10-12, 2016 Kuala Lumpur, Malaysia
International Conference on
Hereditary spastic paraplegias: Identification of a novel SPG57 variant affecting TFG oligomerization and
description of HSP subtypes in Sudan
Ashraf Yahia Osman Mohamed
National University-Sudan, Sudan
Hereditary spastic paraplegias (HSP) are the second most common type of motor neuron disease recognized worldwide. HSP can
be pure or complex according to the absence or presence of additional neurological and non-neurological manifestations. There
are more than 67 known HSP genes with different patterns of inheritance. Autosomal dominant HSP forms are the most frequent
in western populations while recessive HSP predominates in highly consanguineous communities. Our goals were to estimate the
relative frequencies of known HSP genes in Sudanese families with the disease and perform genotype-phenotype correlation to
extend the clinical spectrum associated with HSP genes. We have used next generation sequencing to screen 74 HSP-related genes in
23 consanguineous families from Sudan and candidate gene sequencing in two other families (total of 25 families). We established
a genetic diagnosis in six families with autosomal recessive HSP (SPG11 in three families and TFG/SPG57 , SACS, and ALS2 in one
family each). An autosomal dominant HSP (ATL1/SPG3A) was also identified in one additional family. Six out of seven identified
variants were novel. The TFG/SPG57 variant (p.(Arg22Trp) in the PB1 domain) is the second SPG57 HSP variant to be identified
worldwide, and we demonstrated its impact on TFG oligomerization in vitro. There were no patients with visual impairment as
observed in a previously reported SPG57 family (p. (Arg106Cys) in coiled coil domain), suggesting unique contributions of the PB1
and coiled coil domains in TFG complex formation/function and a possible phenotype correlation to variant location. Some families
manifested marked phenotypic variations implying the possibility of modifier factors complicated by high inbreeding. In conclusion,
we identified the first Sudanese families carrying novel variants in 6 HSP genes. The difficulty to reach a genetic diagnosis in the
majority of studied families suggests the possibility of new genes, unusual models of inheritance or noncoding variations underlying
spinocerebellar degeneration.
In vitro interaction of soluble and amyloid form of serum amyloid protein with amyloid P component to
hepta 1-6 cells
Asokan Chinnasamy and Shagari A B
Sokoto State University, Nigeria
Hepta 1-6 cell binding study is important in relation to the activity of membrane proteins, because losing the activity of such
systems will ultimately lead to malfunction or death of the cell. The interactions of SerumAmyloid A (SAA) and SerumAmyloid
A protofibrils with Serum Amyloid P component [SAP (CaCl2)] to hepta 1-6 cells of the mouse are dealt with in detail to study the
binding of SAA protofibrils in various conditions. The induced fluorescence, circular dichroism, FACScan and MTT assay results
have shown the SAA and SAA fibrils binding with SAP (CaCl2) 0.12-1.2 nM and cell toxicity with the hepta 1-6 cells. Specifically,
interaction of serum amyloid A fibrils with a cell surface binding site/receptor might alter the local environment to cause cellular
dysfunction and to be more favorable for amyloid formation. Already RAGE (receptor for advanced glycation endproducts) a
polyvalent receptor in the immunoglobulin super family has been implicated in binding with the isoform of SAA (SAA1.1) which has
the highest fibirillogenic property. In the present study, SAA fibrils have more binding and cell cytotoxicity than SAA protein and has
protective role with SAP (CaCl2).
Biochem Anal Biochem 2016, 5:3(Suppl)