Unidad 3. Articulos de revision.

Revisiones Generales

Notas a seguir para el desarrollo de las clases.

1. El orden de revisión de los artículos indicados se hará conforme éstos hayan sido presentados a continuación.
2. De los artículos tendrán que tomarse en cuenta varios aspectos: a. Fecha de la publicación. b. Importancia de la revista en la que se hizo la publicación. c. Relación con el desarrollo de la proteómica. d. De los autores indicar el lugar donde actualmente se encuentran laborando y temas de investigación en los que están involucrados (consultar la página web que ellos indiquen). e. Indicar si hay algún trabajo o investigación de relevancia en el campo de la proteómica en el que están trabajndo actualmente los autores de los artículos en revisión.
3. Tomar los aspectos mas relevantes del artículo y presentarlos para discusión. Indicar cual es el motivo por que seleccionaron tal o cual aspecto y que importancia tiene para el campo de la proteómica. Poner especial énfasis en las tablas o gráficos presentados.
4. De los diferentes apartados del blog que se hayan revisado, se hará la presentación de cual fué el motivo de ello y que información relevante se encontro al respecto.

Clase 5 de Agosto

Notas para la clase: Previo a la discusión de los artículos se harán unos ejercicios breves para homogenizar conocimientos generales. Se hará hincapié en todo lo relacionado con aminoácidos (nomenclaturas y propiedades químicas), péptidos (formación y constitución) y proteínas (propiedades químicas, estructuraciones, etc).

Nature. 2000 Jun 15;405(6788):837-46.

Proteomics to study genes and genomes.

Pandey A(1), Mann M.

Proteomics, the large-scale analysis of proteins, will contribute greatly to our 
understanding of gene function in the post-genomic era. Proteomics can be divided
into three main areas: (1) protein micro-characterization for large-scale
identification of proteins and their post-translational modifications; (2)
'differential display' proteomics for comparison of protein levels with potential
application in a wide range of diseases; and (3) studies of protein-protein
interactions using techniques such as mass spectrometry or the yeast two-hybrid
system. Because it is often difficult to predict the function of a protein based 
on homology to other proteins or even their three-dimensional structure,
determination of components of a protein complex or of a cellular structure is
central in functional analysis. This aspect of proteomic studies is perhaps the
area of greatest promise. After the revolution in molecular biology exemplified
by the ease of cloning by DNA methods, proteomics will add to our understanding
of the biochemistry of proteins, processes and pathways for years to come.

Nature. 2003 Mar 13;422(6928):193-7.

From genomics to proteomics.

Tyers M(1), Mann M. Proteomics is the study of the function of all expressed proteins. Tremendous progress has been made in the past few years in generating large-scale data sets for protein-protein interactions, organelle composition, proteinactivity patterns and protein profiles in cancer patients. But further technological improvements, organization of international proteomics projects and open access to results are needed for proteomics to fulfil its potential.

Bischoff R, Schlüter H. Amino acids: chemistry, functionality and selectednon-enzymatic post-translational modifications. J Proteomics. 2012 Apr
18;75(8):2275-96. doi: 10.1016/j.jprot.2012.01.041. Epub 2012 Feb 22. Review.

The ultimate goal of proteomics is determination of the exact chemical composition of protein species, including their complete amino acid sequence and the identification of each modified side chain, in every protein in a biological sample and their quantification. We are still far from achieving this goal due to limitations in analytical methodology and data analysis but also due to the fact that we surely have not discovered all amino acid modifications that occur in nature. To detect modified side chains and to discover new, still unknown amino acid derivatives, an understanding of the chemistry of the reactive groups of amino acids is mandatory. This tutorial focuses on the chemistry of the amino acid side chains and addresses non-enzymatic modifications. By highlighting some exemplary reactions a glimpse of the huge diversity of modified amino acids provides the reader with sufficient insight into amino acid chemistry to raise the awareness for unexpected side chain modifications. We further introduce the reader to a terminology, which enables the comprehensive description of the exact chemical composition of a protein species, including its full amino acid sequence and all modifications of its amino acid side chains. This Tutorial is part of the International Proteomics Tutorial Programme (IPTP number 10).

Clase 9 de Septiembre

Nature. 2014 May 29;509(7502):645-9. doi: 10.1038/509645a. PubMed PMID: 24870547.

Marx V. Proteomics: An atlas of expression. 

The first draft of the complete human proteome has been more than a decade in themaking. In the process, the effort has also delivered lessons about technology and biology.

SCIENTIFIC REPORTS | 4 : 6210 | DOI: 10.1038/srep06210

Microwave & Magnetic (M2) Proteomics Reveals CNS-Specific Protein Expression Waves that Precede Clinical Symptoms of Experimental Autoimmune Encephalomyelitis
Itay Raphael, Swetha Mahesula, Anjali Purkar, David Black, Alexis Catala, Jonathon A. L. Gelfond,Thomas G. Forsthuber & William E. Haskins
Central nervous system-specific proteins (CSPs), transported across the damaged blood-brain-barrier (BBB) to cerebrospinal fluid (CSF) and blood (serum), might bepromising diagnostic, prognostic and predictive protein biomarkers of disease in individual multiple sclerosis (MS) patients because they are not expected to be present at appreciable levels in the circulation of healthy subjects. We hypothesized that microwave & magnetic (M2) proteomics of CSPs in brain tissue might be an effective means to prioritize putative CSP biomarkers for future immunoassays in serum. To test this hypothesis, we used M2 proteomics to longitudinally assess CSP expression in brain tissue from mice during experimental autoimmune encephalomyelitis (EAE), a mouse model of MS. Confirmation of central nervous system (CNS)-infiltrating inflammatory cell response and CSP expression in serum was achieved with cytokine ELISPOT and ELISA immunoassays, respectively, for selected CSPs. M2 proteomics (and ELISA) revealed characteristic CSP expression waves, including synapsin-1 and a-II-spectrin, which peaked at day 7 in brain tissue (and serum)and preceded clinical EAE symptoms that began at day 10 and peaked at day 20. Moreover, M2 proteomics supports the concept that relatively few CNS-infiltrating inflammatory cells can have a disproportionally large impact on CSP expression prior to clinical manifestation of EAE.

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Nat Rev Mol Cell Biol. 2004 Sep;5(9):699-711.

The ABC's (and XYZ's) of peptide sequencing.

Steen H(1), Mann M.

Author information: 
(1)Department of Systems Biology, Harvard Medical School, 240 Longwood Avenue,
Boston, Massachusetts 02115, USA.

Proteomics is an increasingly powerful and indispensable technology in molecular 
cell biology. It can be used to identify the components of small protein
complexes and large organelles, to determine post-translational modifications and
in sophisticated functional screens. The key - but little understood - technology
in mass-spectrometry-based proteomics is peptide sequencing, which we describe
and review here in an easily accessible format.

Science. 2006 Apr 14;312(5771):212-7.

Clase 23 de Septiembre


Müller C, Khabut A, Dudhia J, Reinholt FP, Aspberg A, Heinegård D, Onnerfjord P. Quantitative proteomics at different depths in human articular cartilage reveals unique patterns of protein distribution. Matrix Biol. 2014 Sep 1. pii:S0945-053X(14)00166-8. doi: 10.1016/j.matbio.2014.08.013.[Epub ahead of print]


The articular cartilage of synovial joints ensures friction-free mobility and attenuates mechanical impact on the joint during movement. These functions are mediated by the complex network of extracellular molecules characteristic for articular cartilage. Zonal differences in the extracellular matrix (ECM) are well recognized. However, knowledge about the precise molecular composition in the different zones remains limited. In the present study, we investigated the distribution of ECM molecules along the surface-to-bone axis, using quantitative non-targeted as well as targeted proteomics. In a discovery approach, iTRAQ mass spectrometry was used to identify all extractable ECM proteins in the different layers of a human lateral tibial plateau full thickness cartilage sample. A targeted MRM mass spectrometry approach was then applied to verify these findings and to extend the analysis to four medial tibial plateau samples. In the lateral tibial plateau sample, the unique distribution patterns of 70 ECM proteins were identified, revealing groups of proteins with a preferential distribution to the superficial, intermediate or deep regions of articular cartilage. The detailed analysis of selected 29 proteins confirmed these findings and revealed similar distribution patterns in the four medial tibial plateau samples. The results of this study allow, for the first time, an overview of the zonal distribution of a broad range of cartilage ECM proteins and open up further investigations of the functional roles of matrix proteins in the different zones of articular cartilage in health and disease.

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Mass spectrometry and protein analysis.

Domon B(1), Aebersold R.

Author information: 
(1)Institute of Molecular Systems Biology, ETH Zurich, CH-8093 Zurich, Switzerland.

Mass spectrometry is a central analytical technique for protein research and for 
the study of biomolecules in general. Driven by the need to identify,
characterize, and quantify proteins at ever increasing sensitivity and in ever
more complex samples, a wide range of new mass spectrometry-based analytical
platforms and experimental strategies have emerged. Here we review recent
advances in mass spectrometry instrumentation in the context of current and
emerging research strategies in protein science.

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Microbiología Clínica.

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J Mass Spectrom. 2011 Dec;46(12):1223-32. doi: 10.1002/jms.2008.

Pathogen identification using mass spectrometry in the clinical microbiology
laboratory.

Drake RR(1), Boggs SR, Drake SK.

Author information: 
(1)Department of Pediatrics, Eastern Virginia Medical School, Norfolk, VA 23507,
USA. draker@musc.edu

The recent application of Matrix-assisted Laser Desorption/Ionization
Time-of-Flight and Polymerase Chain Reaction Electrospray Ionization Quadrupole
Time-of-Flight mass spectrometry approaches to microbial identification has
initiated a revolution in the clinical microbiology lab. The commercial
application of these technologies to pathogen identification has only begun in
the last five years, and already new potentially life-saving applications of
these technologies are rapidly identifying organisms that in the past have proven
notoriously difficult to identify. In this review, we will provide a brief
historical perspective on how these developments arose, describe why they are
being successfully applied now and provide an overview of current approaches.
Using examples involving clinical isolates of Staphylococcus aureus, a
perspective on future use and developments of mass spectrometry in the
identification of microbial organisms is provided.

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Nat Rev Microbiol. 2013 Aug;11(8):574-85.

Modern clinical microbiology: new challenges and solutions.

Fournier PE(1), Drancourt M, Colson P, Rolain JM, La Scola B, Raoult D.

Author information: 
(1)Unité de Recherche sur les Maladies Infectieuses et Tropicales Emergentes, UM63, 
CNRS7278, IRD198, INSERMU1095, Marseille, France.

In the twenty-first century, the clinical microbiology laboratory plays a central
part in optimizing the management of infectious diseases and surveying local and 
global epidemiology. This pivotal role is made possible by the adoption of
rational sampling, point-of-care tests, extended automation and new technologies,
including mass spectrometry for colony identification, real-time genomics for
isolate characterization, and versatile and permissive culture systems. When
balanced with cost, these developments can improve the workflow and output of
clinical microbiology laboratories and, by identifying and characterizing
microbial pathogens, provide significant input to scientific discovery.

Clin Chem. 2010 Apr;56(4):525-36. doi: 10.1373/clinchem.2009.138867. Epub 2010
Feb 18.

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Identification of pathogens by mass spectrometry.

Ho YP(1), Reddy PM.

Author information: 
(1)Department of Chemistry, National Dong Hwa University, Hualien, Taiwan.
ypho@mail.ndhu.edu.tw

BACKGROUND: Mass spectrometry (MS) is a suitable technology for microorganism
identification and characterization.
CONTENT: This review summarizes the MS-based methods currently used for the
analyses of pathogens. Direct analysis of whole pathogenic microbial cells using 
MS without sample fractionation reveals specific biomarkers for taxonomy and
provides rapid and high-throughput capabilities. MS coupled with various
chromatography- and affinity-based techniques simplifies the complexity of the
signals of the microbial biomarkers and provides more accurate results.
Affinity-based methods, including those employing nanotechnology, can be used to 
concentrate traces of target microorganisms from sample solutions and, thereby,
improve detection limits. Approaches combining amplification of nucleic acid
targets from pathogens with MS-based detection are alternatives to biomarker
analyses. Many data analysis methods, including multivariate analysis and
bioinformatics approaches, have been developed for microbial identification. The 
review concludes with some current clinical applications of MS in the
identification and typing of infectious microorganisms, as well as some
perspectives.
SUMMARY: Advances in instrumentation (separation and mass analysis), ionization
techniques, and biological methodologies will all enhance the capabilities of MS 
for the analysis of pathogens.

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Paleontología.

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J Proteome Res. 2012 Feb 3;11(2):917-26. doi: 10.1021/pr200721u. Epub 2011 Dec
14.

Proteomic analysis of a pleistocene mammoth femur reveals more than one hundred
ancient bone proteins.

Cappellini E(1), Jensen LJ, Szklarczyk D, Ginolhac A, da Fonseca RA, Stafford TW,
Holen SR, Collins MJ, Orlando L, Willerslev E, Gilbert MT, Olsen JV.

Author information: 
(1)Centre for GeoGenetics, Natural History Museum of Denmark, University of
Copenhagen , Øster Voldgade 5-7, 1350, Copenhagen, Denmark.
ecappellini@googlemail.com

We used high-sensitivity, high-resolution tandem mass spectrometry to shotgun
sequence ancient protein remains extracted from a 43 000 year old woolly mammoth 
( Mammuthus primigenius ) bone preserved in the Siberian permafrost. For the
first time, 126 unique protein accessions, mostly low-abundance extracellular
matrix and plasma proteins, were confidently identified by solid molecular
evidence. Among the best characterized was the carrier protein serum albumin,
presenting two single amino acid substitutions compared to extant African (
Loxodonta africana ) and Indian ( Elephas maximus ) elephants. Strong evidence
was observed of amino acid modifications due to post-mortem hydrolytic and
oxidative damage. A consistent subset of this permafrost bone proteome was also
identified in more recent Columbian mammoth ( Mammuthus columbi ) samples from
temperate latitudes, extending the potential of the approach described beyond
subpolar environments. Mass spectrometry-based ancient protein sequencing offers 
new perspectives for future molecular phylogenetic inference and physiological
studies on samples not amenable to ancient DNA investigation. This approach
therefore represents a further step into the ongoing integration of different
high-throughput technologies for identification of ancient biomolecules,
unleashing the field of paleoproteomics.

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Deportes

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Biochem Biophys Res Commun. 2014 Mar 21;445(4):708-16. doi:
10.1016/j.bbrc.2013.12.137. Epub 2014 Jan 7.

Sportomics: building a new concept in metabolic studies and exercise science.

Bassini A(1), Cameron LC(2).

Author information: 
(1)Laboratory of Protein Biochemistry, Federal University of State of Rio de
Janeiro, Brazil; Brazilian Olympic Committee, Brazil.
(2)Laboratory of Protein Biochemistry, Federal University of State of Rio de
Janeiro, Brazil; Brazilian Olympic Committee, Brazil. Electronic address:
cameron@unirio.br.

For more than a decade, we have used alternative approaches to understand
metabolic responses to physical stress. In addition to classic laboratory studies
(cell and animal models), we have used elite athletes and sports to examine
metabolic stress. Our central question involves the ability of the body to
protect the central nervous system from high and toxic ammonemia during acute and
chronic exercise. Information about this problem can aid in understanding
important signaling pathways, which may yield better ways to protect people who
suffer from diseases that lead to hyperammonemia, such as liver failure, or to
hypermetabolic states, such as cancer or thermal injury. We proposed a Sportomics
approach to mimic the real challenges and conditions that are faced during sports
training and competition. Sportomics is non-hypothesis-driven research on an
individual's metabolite changes during sports and exercise. It is similar to
metabolomics and other "-omics" approaches, but Sportomics focuses on sports as a
metabolic challenge. Our study is holistic and top-down; we treat the data
systematically and have generated a large computer-searchable database. We also
propose that in-field metabolic analyses are important for understanding,
supporting and training elite athletes. In this review, we discuss Sportomics
history, problems, benefits and results. We included different weather
conditions, such as temperature, wind and humidity, and diverse metabolic
responses due to uneven sleep and eating behaviors near the time of the
experiment. We are currently generating databases as well as data-mining
principles and procedures to improve metabolomics and proteomics studies as well 
as adding genomics and transcriptomics studies to the Sportomics approach. We
believe that this approach can fill a methodological gap between systems biology 
and translational medicine similar as a bench to the field approach.

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Biología Celular

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Parasitol Res. 2014 May;113(5):1955-69. doi: 10.1007/s00436-014-3846-4. Epub 2014
Mar 21.

Analysis of the expression of cytoskeletal proteins of Taenia crassiceps ORF
strain cysticerci (Cestoda).

Reynoso-Ducoing O(1), Valverde-Islas L, Paredes-Salomon C, Pérez-Reyes A, Landa
A, Robert L, Mendoza G, Ambrosio JR.

Author information: 
(1)Facultad de Medicina, Departamento de Microbiología y Parasitología, Universidad 
Nacional Autónoma de México, 04510, México, DF, México.

The Taenia crassiceps ORF strain is used to generate a murine model of
cysticercosis, which is used for diagnosis, evaluation of drugs, and vaccination.
This particular strain only exists as cysticerci, is easily maintained under in
vivo and in vitro conditions, and offers an excellent model for studying the
cytoskeletons of cestodes. In this study, several experimental approaches were
used to determine the tissue expression of its cytoskeletal proteins. The
techniques used were microscopy (video, confocal, and transmission electron),
one-dimensional (1D) and two-dimensional (2D) electrophoresis, immunochemistry,
and mass spectrometry. The tissue expression of actin, tubulin, and paramyosin
was assessed using microscopy, and their protein isoforms were determined with 1D
and 2D electrophoresis and immunochemistry. Nineteen spots were excised from a
proteomic gel and identified by liquid chromatography-tandem mass spectrometry
and immunochemistry. The proteins identified were classic cytoskeletal proteins, 
metabolic enzymes, and proteins with diverse biological functions, but mainly
involved in detoxification activities. Research suggests that most
noncytoskeletal proteins interact with actin or tubulin, and the results of the
present study suggest that the proteins identified may be involved in supporting 
the dynamics and plasticity of the cytoskeleton of T. crassiceps cysticerci.
These results contribute to our knowledge of the cellular biology and physiology 
of cestodes.

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2. Int J Parasitol. 2014 May 28. pii: S0020-7519(14)00112-X. doi:
10.1016/j.ijpara.2014.04.004. [Epub ahead of print]

Oestradiol and progesterone differentially alter cytoskeletal protein expression 
and flame cell morphology in Taenia crassiceps.

Ambrosio JR(1), Ostoa-Saloma P(2), Palacios-Arreola MI(2), Ruíz-Rosado A(2),
Sánchez-Orellana PL(3), Reynoso-Ducoing O(1), Nava-Castro KE(4),
Martínez-Velázquez N(2), Escobedo G(5), Ibarra-Coronado EG(2), Valverde-Islas
L(1), Morales-Montor J(6).

Author information: 
(1)Departamento de Microbiología y Parasitología, Facultad de Medicina, Universidad 
Nacional Autónoma de México, Edificio A, 2do piso, Ciudad Universitaria, México
DF 04510, Mexico.
(2)Departamento de Inmunología, Instituto de Investigaciones Biomédicas, Universidad
Nacional Autónoma de México, AP 70228, México DF 04510, Mexico.
(3)Departamento de Fisiología Biofísica y Neurociencias, CINVESTAV-IPN, Av.
Instituto Politecnico Nacional 2508, San Pedro Zacatenco, Gustavo A. Madero,
México DF 07360, Mexico.
(4)Centro de investigación sobre enfermedades infecciosas, Instituto Nacional de
Salud Pública, 62100 Cuernavaca, Morelos, Mexico.
(5)Unidad de Medicina Experimental, Hospital General de México, AP 06726, México DF,
Mexico.
(6)Departamento de Inmunología, Instituto de Investigaciones Biomédicas, Universidad
Nacional Autónoma de México, AP 70228, México DF 04510, Mexico. Electronic
address: jmontor66@hotmail.com.

We examined the effects of oestradiol (E2) and progesterone (P4) on cytoskeletal 
protein expression in the helminth Taenia crassiceps - specifically actin,
tubulin and myosin. These proteins assemble into flame cells, which constitute
the parasite excretory system. Total protein extracts were obtained from E2- and 
P4-treated T. crassiceps cysticerci and untreated controls, and analysed by one- 
and two-dimensional protein electrophoresis, flow cytometry, immunofluorescence
and videomicroscopy. Exposure of T. crassiceps cysticerci to E2 and P4 induced
differential protein expression patterns compared with untreated controls.
Changes in actin, tubulin and myosin expression were confirmed by flow cytometry 
of parasite cells and immunofluorescence. In addition, parasite morphology was
altered in response to E2 and P4 versus controls. Flame cells were primarily
affected at the level of the ciliary tuft, in association with the changes in
actin, tubulin and myosin. We conclude that oestradiol and progesterone act
directly on T. crassiceps cysticerci, altering actin, tubulin and myosin
expression and thus affecting the assembly and function of flame cells. Our
results increase our understanding of several aspects of the molecular crosstalk 
between host and parasite, which might be useful in designing anthelmintic drugs 
that exclusively impair parasitic proteins which mediate cell signaling and
pathogenic reproduction and establishment.

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3. Cell Biol Int. 2003;27(9):727-33.

Actin expression in Taenia solium cysticerci (cestoda): tisular distribution and 
detection of isoforms.

Ambrosio JR(1), Reynoso-Ducoing O, Hernández-Sanchez H, Correa-Piña D,
González-Malerva L, Cruz-Rivera M, Flisser A.

Author information: 
(1)Facultad de Medicina, Universidad Nacional Autónoma de México, Edificio A, 2o
Piso, Circ. Int. Cd. Universitaria, D.F. 04510 Mexico, Mexico.
jrah@servidor.unam.mx

Identification, localization and partial biochemical characterization of actins
expressed in the larval stage of the cestode parasite Taenia solium has been
carried out. Frozen tissue sections of cysticerci, the larval stage of this
parasite, were reacted with rhodamine-phalloidin, parasite actin was purified by 
polymerization in the presence of K(+), Mg(++) and ATP actin was analyzed by
SDS-PAGE and two-dimensional gel electrophoresis, and immunoblotting of actin was
performed in PVDF membranes and with commercial anti-actin monoclonal antibodies.
Parasitic tissues showed different fibrous actin fluorescence patterns, which
correlated with the expression of isoactins. Purified globular actin had a
similar molecular mass to rabbit commercial actin (approximately 44 kDa). Actin
was resolved into seven isoforms, indicating a family of actin genes.

J Proteomics. 2014 Mar 21. pii: S1874-3919(14)00130-4. doi:

10.1016/j.jprot.2014.03.008. [Epub ahead of print]

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Proteomic characterization of the subpellicular cytoskeleton of Toxoplasma gondii
tachyzoites.

Gómez de León CT(1), Díaz Martín RD(1), Mendoza Hernández G(2), González Pozos
S(3), Ambrosio JR(4), Mondragón Flores R(5).

Author information: 
(1)Departamento de Bioquímica, Centro de Investigación y Estudios Avanzados del
Instituto Politécnico Nacional (CINVESTAV-IPN), Av. IPN #2508 Del. G. A. Madero, 
Col. Zacatenco, C.P. 07360, México D.F., México.
(2)Departamento de Bioquímica, Facultad de Medicina, Universidad Nacional Autónoma
de México (UNAM), C.P. 04510, México, D.F., México.
(3)Unidad de Microscopía Electrónica (LaNSE), CINVESTAV-IPN, México.
(4)Departamento de Microbiología y Parasitología, Facultad de Medicina, UNAM, C.P.
04510, México D.F., México.
(5)Departamento de Bioquímica, Centro de Investigación y Estudios Avanzados del
Instituto Politécnico Nacional (CINVESTAV-IPN), Av. IPN #2508 Del. G. A. Madero, 
Col. Zacatenco, C.P. 07360, México D.F., México. Electronic address:
rmflores@cinvestav.mx.

Toxoplasma, the causative agent of toxoplasmosis in animals and humans, has a
subpellicular cytoskeleton that is involved in motility, cell shape and invasion.
Knowledge of components of the cytoskeleton is necessary to understand the
invasion mechanisms as well as for the identification of possible therapeutic
targets. To date, most cytoskeletal components of Toxoplasma remain unidentified 
due mainly to the lack of reproducible methods for their isolation. Based on the 
successful isolation of the cytoskeleton, it was possible to report for the first
time, the proteomic characterization of the subpellicular cytoskeleton of
Toxoplasma formed by 95 cytoskeletal proteins through proteomic analysis by
tandem mass spectrometry of one dimension SDS PAGE. By bioinformatic analysis of 
the data, proteins were classified as: 18 conventional cytoskeletal proteins; 10 
inner membrane complex proteins, including 7 with alveolin repeats; 5 new
proteins with alveolin like repeats; 37 proteins associated with other organelles
and 25 novel proteins of unknown function. One of the alveolin like proteins not 
previously described in Toxoplasma named TgArticulin was partially characterized 
with a specific monoclonal antibody. Presence of TgArticulin was exclusively
associated with the cytoskeleton fraction with a cortical distribution. Functions
for the several molecules identified are proposed.BIOLOGICAL SIGNIFICANCE: This
manuscript describes, for the first time, the proteome of the subpellicular
cytoskeleton of Toxoplasma gondii. The importance of this study is related to the
role of the cytoskeleton in the highly invasive capability of a parasite that
causes abortion, blindness, and death by encephalitis in immunocompromised
patients. Proteomic characterization of the cytoskeleton of T. gondii tachyzoites
was possible by the development of a successful procedure for the isolation of
the subpellicular cytoskeleton. Knowledge of the composition of the cytoskeleton 
of Toxoplasma is fundamental for the understanding of the motility and host cell 
invasion mechanisms, and for the future design and development of toxoplasmicidal
drugs with effects against specific components of the cytoskeleton of this
parasite that are absent in mammal host cells. This article is part of a Special 
Issue entitled: Proteomics, mass spectrometry and peptidomics, Cancun 2013.

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Inmunología

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Diaz-Masmela Y, Fragoso G, Ambrosio JR, Mendoza-Hernández G, Rosas G, Estrada 
K, Carrero JC, Sciutto E, Laclette JP, Bobes RJ. Immunodiagnosis of porcine
cysticercosis: identification of candidate antigens through immunoproteomics. Vet
J. 2013 Dec;198(3):656-60.