User:Cedombroski/sandbox

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Practice[edit]

This is my sandbox page. I am currently learning to use wiki markup.

This is bold formatting.

Article Evaluation[edit]

  • Everything is relevant to the topic, however the organization of the major and minor diseases could do with different formatting.
  • The article is neutral.
  • The links available work, but there are some paragraphs with claims that do not have any citations.
  • The talk page gives suggestions as to how to improve the organization and content of the article, as well as suggestions of other topics to add.

Article Selection[edit]

-These all seems like viable options. CHoose the one that interests you most. Be mindful of not getting repetitive on the AMH receptor page with information about AMH itself. - Dr. Tienson-Tseng

Bibliography[edit]

I will choose the article that has the most amount of comprehensive and reliable sources

Growth-hormone-releasing hormone receptor

  • Endocrinology textbooks?
  • Human Growth Hormone Research and Clinical Practice

Merozoite surface protein

  • Microbiology/Parasitology textbooks?
  • N-Terminal Plasmodium vivax Merozoite Surface Protein-1, a Potential Subunit for Malaria Vivax Vaccine[1]
    • Very comprehensive information
  • Merozoite surface proteins in red blood cell invasion, immunity and vaccines against malaria.[2]
    • Excellent summary of proteins and their role
  • Suramin & suramin analogues inhibit merozoite surface protein-1 secondary processing and erythrocyte invasion by the malaria parasite Plasmodium falciparum.[3]
    • Primary literature, but very comprehensive info about mechanisms
  • Designing malaria vaccines to circumvent antigen variability.[4]
    • Mentions current vaccines that make use of MSPs
  • The carboxy-terminus of merozoite surface protein 1: structure, specific antibodies and immunity to malaria.[5]
    • Good background info on MSP-1
  • Signaling Strategies of Malaria Parasite for Its Survival, Proliferation, and Infection during Erythrocytic Stage.[6]
    • Nice figures for understanding mechanism
  • A single fragment of a malaria merozoite surface protein remains on the parasite during red cell invasion and is the target of invasion-inhibiting antibodies.[7]
    • Reviews interaction with RBCs
  • Analysis of sequence diversity in the Plasmodium falciparum merozoite surface protein-1 (MSP-1).[8]
    • Reviews vaccine trials and effectiveness in primates
  • No free article available, but come up often in PubMed searches
    • Molecular Signaling Involved in Entry and Exit of Malaria Parasites from Host Erythrocytes.[9]
    • Merozoite surface protein 1, immune evasion, and vaccines against asexual blood stage malaria.
    • Genetic diversity in Plasmodium falciparum merozoite surface protein 1 and 2 coding genes and its implications in malaria epidemiology: a review of published studies from 1997-2007.
  • Merozoite surface proteins of the malaria parasite: The MSP1 complex and the MSP7 family[10]
    • Citation of the original article
  • Macrolides rapidly inhibit red blood cell invasion by the human malaria parasite, Plasmodium falciparum.[11]
    • Drug development that targets MSPs (an alternative to creating vaccines)
  • NCBI gene information
  • MSP-1 Primary sequence diagram

I found these sources and think that they provide comprehensive information that would improve this article. Any feedback would be welcome

  • N-Terminal Plasmodium vivax Merozoite Surface Protein-1, a Potential Subunit for Malaria Vivax Vaccine[1]
  • Merozoite surface proteins in red blood cell invasion, immunity and vaccines against malaria.[2]
  • Suramin & suramin analogues inhibit merozoite surface protein-1 secondary processing and erythrocyte invasion by the malaria parasite Plasmodium falciparum.[3]
  • Designing malaria vaccines to circumvent antigen variability.[4]
  • The carboxy-terminus of merozoite surface protein 1: structure, specific antibodies and immunity to malaria.[5]
  • Signaling Strategies of Malaria Parasite for Its Survival, Proliferation, and Infection during Erythrocytic Stage.[6]
Merozoite Surface Protein-1
Identifiers
OrganismPlasmodium falciparum 3D7
SymbolMSP-1
Alt. symbolsPF3D7_0930300 [12]
PDB2MGP, 2MGR, 2NPR, 2FLG, 1N1I, 1CEJ, 1B9W 2MUE, 2MGP, 2MGR, 2NPR, 2FLG, 1N1I, 1CEJ, 1B9W
Other data
Chromosome9: 1.2 - 1.21 Mb

Merozoite Surface Protein (Rough Draft)[edit]

Merozoite /ˌmɛrəˈzˌt/ surface proteins are both integral and peripheral membrane proteins found on the surface of a merozoite, an early life cycle stage of a protozoan.[10] Merozoite surface proteins, or MSPs, are important in understanding malaria, a disease caused by protozoans of the genus Plasmodium. During the asexual blood stage of its life cycle, the malaria parasite enters red blood cells to replicate itself, causing the classic symptoms of malaria.[9] These surface protein complexes are involved in many interactions of the parasite with red blood cells and are therefore an important topic of study for scientists aiming to combat malaria.[2]

The MSP-1 complex is attached to the merozoite cell membrane via GPI-anchoring, indicated by the staggered lines penetrating the cell membrane. After red blood cell invasion the majority of the MSP-1 complex is shed, leaving MSP-119 behind.[10]
The relative size and location of each segment of the primary structure of on MSP-1 complex is shown above. SS represents the signal sequence, which is a short sequence present on the N-terminus of new proteins. GA represents the GPI anchor, which is located at the C-terminus of the protein.[13]

Forms and Function[edit]

The most common form of MSPs are anchored to the merozoite surface with glycophosphatidylinositol, a short glycolipid often used for protein anchoring. Additional forms include integral membrane proteins and peripherally associated proteins, which are found to a lesser extent than glycophosphatidylinositol anchored proteins, or (GPI)-anchored proteins, on the merozoite surface.[2] Merozoite surface proteins 1 and 2 are the most abundant (GPI)-anchored proteins on the surface of Plasmodium merozoites.[2] MSP-1 is synthesized at the very beginning of schizogony, or asexual merozoite reproduction.[5] The merozoite first attaches to a red blood cell using its MSP-1 complex. The MSP-1 complex targets spectrin, a complex on the internal surface of the cell membrane of a red blood cell. The majority of the MSP-1 complex is shed upon entry into the red blood cell, but a small portion of the C-terminus, called MSP-119, is conserved.[7] The exact role of MSP-119 remains unknown, but it serves as a marker for the formation of the food vacuole.[10] The function of the MSP-2 complex is not concrete, but current research suggests it has a role in red blood cell invasion due to its degradation shortly after invasion.[2] MSP- 3, 6, 7 and 9 are peripheral membrane proteins that have been shown to form a complex with MSP-1, but the functions of these proteins are largely unknown. [2]

Clinical Significance[edit]

Due to their prevalence on the Plasmodium surface, MSPs have been a key target for vaccine development. Anti-malarial vaccines have been developed to target the merozoite at different stages in its life cycle. Vaccines that target the merozoite in its asexual erythrocytic stage utilize merozoite surface proteins, particularly MSP-1.[1] The biggest challenge faced when developing these vaccines is the high complexity and variation of these proteins. In merozoites of the same genus and species, the sequences encoding proteins such as MSP-1 vary greatly depending on the region they are found. [8] For example, the Combination B vaccine utilizes antigens of MSP-1 and MSP-2 but has limited efficacy based primarily on the MSP-2 alleles used.[4] In an attempt to increase the efficiency of vaccines produced, constant regions such as MSP-119 which remain on the surface of the Plasmodium after the merozoite stage are becoming a key focus for vaccine studies.[2] Additionally, synthetic glycophosphatidylinositol (GPI) molecules are emerging as a potential candidate due to their ability to elicit a strong immune response while simultaneously remaining relatively consistent in structure throughout various malarial strains.[6]

In addition to vaccines, researchers are developing drugs that bind to MSPs in order to disrupt merozoite replication.[11] Suramin, a drug used to treat African sleeping sickness, has shown moderate success with binding to MSP-1 and its derivatives such as MSP-119 to inhibit red blood cell invasion.[3]

References[edit]

  1. ^ a b c Versiani, Fernanda G.; Almeida, Maria E.; Mariuba, Luis A.; Orlandi, Patricia P.; Nogueira, Paulo A. (2013). "N-terminal Plasmodium vivax merozoite surface protein-1, a potential subunit for malaria vivax vaccine". Clinical & Developmental Immunology. 2013: 965841. doi:10.1155/2013/965841. ISSN 1740-2530. PMC 3804292. PMID 24187566.{{cite journal}}: CS1 maint: PMC format (link) CS1 maint: unflagged free DOI (link)
  2. ^ a b c d e f g h Beeson, James G.; Drew, Damien R.; Boyle, Michelle J.; Feng, Gaoqian; Fowkes, Freya J.I.; Richards, Jack S. (2016-01-31). "Merozoite surface proteins in red blood cell invasion, immunity and vaccines against malaria". FEMS Microbiology Reviews. 40 (3): 343–372. doi:10.1093/femsre/fuw001. ISSN 1574-6976.
  3. ^ a b c Fleck, Suzanne L.; Birdsall, Berry; Babon, Jeffrey; Dluzewski, Anton R.; Martin, Stephen R.; Morgan, William D.; Angov, Evelina; Kettleborough, Catherine A.; Feeney, James (2003-11-28). "Suramin and suramin analogues inhibit merozoite surface protein-1 secondary processing and erythrocyte invasion by the malaria parasite Plasmodium falciparum". The Journal of Biological Chemistry. 278 (48): 47670–47677. doi:10.1074/jbc.M306603200. ISSN 0021-9258. PMID 13679371.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  4. ^ a b c Ouattara, Amed; Barry, Alyssa E.; Dutta, Sheetij; Remarque, Edmond J.; Beeson, James G.; Plowe, Christopher V. (2015-12-22). "Designing malaria vaccines to circumvent antigen variability". Vaccine. 33 (52): 7506–7512. doi:10.1016/j.vaccine.2015.09.110. ISSN 1873-2518. PMC 4731100. PMID 26475447.{{cite journal}}: CS1 maint: PMC format (link)
  5. ^ a b c Holder, A. A. (2009-07-23). "The carboxy-terminus of merozoite surface protein 1: structure, specific antibodies and immunity to malaria". Parasitology. 136 (12): 1445–1456. doi:10.1017/S0031182009990515. ISSN 1469-8161. PMID 19627632.
  6. ^ a b c Soni, Rani; Sharma, Drista; Rai, Praveen; Sharma, Bhaskar; Bhatt, Tarun K. (2017). "Signaling Strategies of Malaria Parasite for Its Survival, Proliferation, and Infection during Erythrocytic Stage". Frontiers in Immunology. 8: 349. doi:10.3389/fimmu.2017.00349. ISSN 1664-3224. PMC 5368685. PMID 28400771.{{cite journal}}: CS1 maint: PMC format (link) CS1 maint: unflagged free DOI (link)
  7. ^ a b Blackman, M. J.; Heidrich, H. G.; Donachie, S.; McBride, J. S.; Holder, A. A. (1990-07-01). "A single fragment of a malaria merozoite surface protein remains on the parasite during red cell invasion and is the target of invasion-inhibiting antibodies". The Journal of Experimental Medicine. 172 (1): 379–382. ISSN 0022-1007. PMC 2188181. PMID 1694225.{{cite journal}}: CS1 maint: PMC format (link)
  8. ^ a b Miller, L. H.; Roberts, T.; Shahabuddin, M.; McCutchan, T. F. (1993-5). "Analysis of sequence diversity in the Plasmodium falciparum merozoite surface protein-1 (MSP-1)". Molecular and Biochemical Parasitology. 59 (1): 1–14. ISSN 0166-6851. PMID 8515771. {{cite journal}}: Check date values in: |date= (help)
  9. ^ a b Singh, Shailja; Chitnis, Chetan E. (2017-10-03). "Molecular Signaling Involved in Entry and Exit of Malaria Parasites from Host Erythrocytes". Cold Spring Harbor Perspectives in Medicine. 7 (10). doi:10.1101/cshperspect.a026815. ISSN 2157-1422. PMC 5629987. PMID 28507195.{{cite journal}}: CS1 maint: PMC format (link)
  10. ^ a b c d Kadekoppala, Madhusudan; Holder, Anthony A. (2010-08). "Merozoite surface proteins of the malaria parasite: The MSP1 complex and the MSP7 family". International Journal for Parasitology. 40 (10): 1155–1161. doi:10.1016/j.ijpara.2010.04.008. ISSN 0020-7519. {{cite journal}}: Check date values in: |date= (help)
  11. ^ a b Wilson, Danny W.; Goodman, Christopher D.; Sleebs, Brad E.; Weiss, Greta E.; de Jong, Nienke Wm; Angrisano, Fiona; Langer, Christine; Baum, Jake; Crabb, Brendan S. (2015-07-18). "Macrolides rapidly inhibit red blood cell invasion by the human malaria parasite, Plasmodium falciparum". BMC biology. 13: 52. doi:10.1186/s12915-015-0162-0. ISSN 1741-7007. PMC 4506589. PMID 26187647.{{cite journal}}: CS1 maint: PMC format (link) CS1 maint: unflagged free DOI (link)
  12. ^ "PF3D7_0930300 merozoite surface protein 1 [Plasmodium falciparum 3D7] - Gene - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2018-11-26.
  13. ^ Woehlbier, Ute; Epp, Christian; Hackett, Fiona; Blackman, Michael J.; Bujard, Hermann (2010-03-18). "Antibodies against multiple merozoite surface antigens of the human malaria parasite Plasmodium falciparum inhibit parasite maturation and red blood cell invasion". Malaria Journal. 9 (1): 77. doi:10.1186/1475-2875-9-77. ISSN 1475-2875. PMC 2847572. PMID 20298576.{{cite journal}}: CS1 maint: unflagged free DOI (link)