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You searched for subject:(GAL102 Biochemical Characterization). Showing records 1 – 2 of 2 total matches.

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Indian Institute of Science

1. Sen, Manimala. Identification Of GAL102 Encoded UDP-Glucose 4, 6 Dehydratase Activity, As A Novel Virulence Factor In Candida Albicans.

Degree: 2011, Indian Institute of Science

Among fungal pathogens responsible for opportunistic infections, species of the genus Candida have a major role (Mitchell, 1998). Various Candida species cause superficial infections which can be cured by the currently available antifungal arsenal (Noble and Johnson, 2007). However, species of the genus Candida are also responsible for life-threatening systemic infections, particularly in immunocompromised patients with weakened immune system. Among Candida species, C. albicans, which can also be a commensal of the skin and the gastrointestinal and genitourinary tracts, is responsible for the majority of Candida bloodstream infections. However, there is an increasing incidence of infections caused by C. glabrata because it is less susceptible to azoles. Other medically important Candida species include C. parapsilosis, C. tropicalis and C. dubliniensis. The problem has been further worsened by the emergence of many drug resistant isolates which pose a major hurdle during a given treatment regimen. Therefore, there is a dire need to identify novel drug targets and the current study focuses on one such protein found in C. albicans and related Candida species. CaGAL102 does not encode a functional galactose epimerase CaGAL102 was previously identified in the lab as a paralog of CaGAL10. CaGAL10 endoes a functional UDP-galactose 4-epimerase and it can complement a Scgal10 null strain. Further, work on the Gal10 protein in the encapsulated yeast Cryptococcus neoformans identified two Gal10 paralogs in the genome, Uge1 and Uge2 with distinct functions (Moyrand et al., 2008). A similar scenario is found in S. pombe in which two Gal10 sequence homologs have been annotated. In the light of these observations, we wanted to test if CaGAL102 also encodes a functional ScGAL10 homolog. We found that CaGAL102 could not complement Scgal10 null strain though there was a strong conservation in the cofactor and the catalytic motif in both the proteins. We found after a careful literature review that Gal10 belongs to a family of proteins called the short chain dehydratase/reductase family (SDR) (Jornvall et al., 1995), members of which are characterised by the presence of glycine rich cofactor binding motif at the N-terminus and an YXXXK catalytic motif. Proteins belonging to the SDR family have a residue level identity of 15-30% indicating early duplication and divergence. Based on our literature survey we carried out a BLAST search in the NCBI protein database using CaGal102 as the bait protein. We found that CaGal102 is 32% identical at the protein level to dTDP-glucose 4,6 dehydratase (RmlB), another member of the SDR family. RmlB is the second enzyme of the rhamnose biosynthetic pathway which gives rise to dTDP-rhamnose. This pathway is involved in cell wall biosynthesis in bacteria and it has been shown that rmlB is essential for growth of Mycobacterium smegmatis (Li et al, 2006). Interestingly rhamnose is not present in the cell wall of C. albicans. Biochemical characterisation of CaCaGal102 A plant homolog of RmlB is… Advisors/Committee Members: Sadhale, Parag P.

Subjects/Keywords: Fungal Diseases - Proteins - Characterization; Candida albicans (Fungus); GAL102 (Proteins); Fungal Pathogens; GAL102 - Biochemical Characterization; C. albicans; Mycology

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Sen, M. (2011). Identification Of GAL102 Encoded UDP-Glucose 4, 6 Dehydratase Activity, As A Novel Virulence Factor In Candida Albicans. (Thesis). Indian Institute of Science. Retrieved from http://hdl.handle.net/2005/2364

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16th Edition):

Sen, Manimala. “Identification Of GAL102 Encoded UDP-Glucose 4, 6 Dehydratase Activity, As A Novel Virulence Factor In Candida Albicans.” 2011. Thesis, Indian Institute of Science. Accessed January 17, 2020. http://hdl.handle.net/2005/2364.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7th Edition):

Sen, Manimala. “Identification Of GAL102 Encoded UDP-Glucose 4, 6 Dehydratase Activity, As A Novel Virulence Factor In Candida Albicans.” 2011. Web. 17 Jan 2020.

Vancouver:

Sen M. Identification Of GAL102 Encoded UDP-Glucose 4, 6 Dehydratase Activity, As A Novel Virulence Factor In Candida Albicans. [Internet] [Thesis]. Indian Institute of Science; 2011. [cited 2020 Jan 17]. Available from: http://hdl.handle.net/2005/2364.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Sen M. Identification Of GAL102 Encoded UDP-Glucose 4, 6 Dehydratase Activity, As A Novel Virulence Factor In Candida Albicans. [Thesis]. Indian Institute of Science; 2011. Available from: http://hdl.handle.net/2005/2364

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation


Indian Institute of Science

2. Sen, Manimala. Identification Of GAL102 Encoded UDP-Glucose 4, 6 Dehydratase Activity, As A Novel Virulence Factor In Candida Albicans.

Degree: 2011, Indian Institute of Science

Among fungal pathogens responsible for opportunistic infections, species of the genus Candida have a major role (Mitchell, 1998). Various Candida species cause superficial infections which can be cured by the currently available antifungal arsenal (Noble and Johnson, 2007). However, species of the genus Candida are also responsible for life-threatening systemic infections, particularly in immunocompromised patients with weakened immune system. Among Candida species, C. albicans, which can also be a commensal of the skin and the gastrointestinal and genitourinary tracts, is responsible for the majority of Candida bloodstream infections. However, there is an increasing incidence of infections caused by C. glabrata because it is less susceptible to azoles. Other medically important Candida species include C. parapsilosis, C. tropicalis and C. dubliniensis. The problem has been further worsened by the emergence of many drug resistant isolates which pose a major hurdle during a given treatment regimen. Therefore, there is a dire need to identify novel drug targets and the current study focuses on one such protein found in C. albicans and related Candida species. CaGAL102 does not encode a functional galactose epimerase CaGAL102 was previously identified in the lab as a paralog of CaGAL10. CaGAL10 endoes a functional UDP-galactose 4-epimerase and it can complement a Scgal10 null strain. Further, work on the Gal10 protein in the encapsulated yeast Cryptococcus neoformans identified two Gal10 paralogs in the genome, Uge1 and Uge2 with distinct functions (Moyrand et al., 2008). A similar scenario is found in S. pombe in which two Gal10 sequence homologs have been annotated. In the light of these observations, we wanted to test if CaGAL102 also encodes a functional ScGAL10 homolog. We found that CaGAL102 could not complement Scgal10 null strain though there was a strong conservation in the cofactor and the catalytic motif in both the proteins. We found after a careful literature review that Gal10 belongs to a family of proteins called the short chain dehydratase/reductase family (SDR) (Jornvall et al., 1995), members of which are characterised by the presence of glycine rich cofactor binding motif at the N-terminus and an YXXXK catalytic motif. Proteins belonging to the SDR family have a residue level identity of 15-30% indicating early duplication and divergence. Based on our literature survey we carried out a BLAST search in the NCBI protein database using CaGal102 as the bait protein. We found that CaGal102 is 32% identical at the protein level to dTDP-glucose 4,6 dehydratase (RmlB), another member of the SDR family. RmlB is the second enzyme of the rhamnose biosynthetic pathway which gives rise to dTDP-rhamnose. This pathway is involved in cell wall biosynthesis in bacteria and it has been shown that rmlB is essential for growth of Mycobacterium smegmatis (Li et al, 2006). Interestingly rhamnose is not present in the cell wall of C. albicans. Biochemical characterisation of CaCaGal102 A plant homolog of RmlB is… Advisors/Committee Members: Sadhale, Parag P.

Subjects/Keywords: Fungal Diseases - Proteins - Characterization; Candida albicans (Fungus); GAL102 (Proteins); Fungal Pathogens; GAL102 - Biochemical Characterization; C. albicans; Mycology

Record DetailsSimilar RecordsGoogle PlusoneFacebookTwitterCiteULikeMendeleyreddit

APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Sen, M. (2011). Identification Of GAL102 Encoded UDP-Glucose 4, 6 Dehydratase Activity, As A Novel Virulence Factor In Candida Albicans. (Thesis). Indian Institute of Science. Retrieved from http://etd.iisc.ernet.in/handle/2005/2364 ; http://etd.ncsi.iisc.ernet.in/abstracts/3038/G24992-Abs.pdf

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16th Edition):

Sen, Manimala. “Identification Of GAL102 Encoded UDP-Glucose 4, 6 Dehydratase Activity, As A Novel Virulence Factor In Candida Albicans.” 2011. Thesis, Indian Institute of Science. Accessed January 17, 2020. http://etd.iisc.ernet.in/handle/2005/2364 ; http://etd.ncsi.iisc.ernet.in/abstracts/3038/G24992-Abs.pdf.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7th Edition):

Sen, Manimala. “Identification Of GAL102 Encoded UDP-Glucose 4, 6 Dehydratase Activity, As A Novel Virulence Factor In Candida Albicans.” 2011. Web. 17 Jan 2020.

Vancouver:

Sen M. Identification Of GAL102 Encoded UDP-Glucose 4, 6 Dehydratase Activity, As A Novel Virulence Factor In Candida Albicans. [Internet] [Thesis]. Indian Institute of Science; 2011. [cited 2020 Jan 17]. Available from: http://etd.iisc.ernet.in/handle/2005/2364 ; http://etd.ncsi.iisc.ernet.in/abstracts/3038/G24992-Abs.pdf.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Sen M. Identification Of GAL102 Encoded UDP-Glucose 4, 6 Dehydratase Activity, As A Novel Virulence Factor In Candida Albicans. [Thesis]. Indian Institute of Science; 2011. Available from: http://etd.iisc.ernet.in/handle/2005/2364 ; http://etd.ncsi.iisc.ernet.in/abstracts/3038/G24992-Abs.pdf

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

.