Recent Research: Experimental Applications of Pertussis Toxin and Cholera Toxin

The List Labs Citation Database is a robust tool for researchers. It offers thousands of papers showing how List Labs products are used experimentally. Researchers can search for keywords specific to their fields of study and learn how others in that field have used our toxins and antigens.

In this article, we will explore experimental applications for two of our most popular products: Pertussis Toxin (Products #180, #181 and #184) and Cholera Toxin (Product #100B). This article is not exhaustive – we will focus on recent research – but it offers a survey of ways in which List Labs is helping to get science done.

Pertussis Toxin Applications

Experimental autoimmune encephalomyelitis (EAE) is an induced autoinflammatory condition of the central nervous system. It is used in rodents as a model of demyelinating diseases such as multiple sclerosis and of T-cell-mediated autoimmune disease in general. Inducing EAE usually uses isolated myelin proteins or homogenate along with pertussis toxin to open the blood-brain barrier and allow T-cells access to the CNS. Many citations in the database note this use of those products.

But that’s far from the only way researchers have found to use List Labs’ pertussis toxin. An international team of researchers found that pertussis toxin reduces cellular damage following ischemic strokes. Another used it in their study of myocarditis. A Michigan team used pertussis toxin to develop an innovative high-molecular-weight mass spectrometry application. And of course several research groups used it developing assays and treatments for whooping cough.

Cholera Toxin Applications

The applications for cholera toxin are equally diverse. Besides treatments for cholera, researchers recently used the toxin to study the role of bone morphogenetic proteins and mesenchymal stem cells in breast cancer, as well as TRAIL therapy to treat such cancers. Other cancer researchers looked at hemocyanin as a treatment for bladder cancer, using List’s cholera toxin.

Investigators studied vaccines against Helicobacter pylori, which is known to cause peptic ulcers and is a risk factor for gastric cancer.

Food allergies are a serious and growing problem. Our citation database lists studies that used cholera toxin to aid in the study of allergies to several common foods (especially peanuts). Cholera toxin was also studied as an adjuvant for intranasal vaccines and used to investigate the role of immunoglobulin E (IgE) in anaphylactic shock—an extreme and potentially fatal allergic reaction.

Cholera toxin was even used to study the cellular mechanisms of Yersinia pestis, the pathogen that causes bubonic plague.

This is only a brief survey of recent research using two of List Labs’ more popular products. It illustrates both the wide range of applications for List’s bacterial toxins and the utility of the List citation database as a tool to facilitate your literature surveys.

List Labs offers citations on our website for easy use by researchers. At present we have over 3,000 citations from publications around the world, with emphasis on the last 5 years. We provide information on how to purchase the referenced products and the ability to sort from among the over 100 catalog items we offer here.

We are very appreciative of the work done using our products and the many ways they have been featured in research that’s potentially instrumental in changing the world.

We have gathered citations for our Pertussis product group. We hope you enjoy this infographic and find it useful.

List Labs Pertussis toxins for research:

List Biological Laboratories provides B. pertussis virulence factors: Pertussis Toxin, Pertussis Toxin Subunits, Filamentous Hemagglutinin (FHA), Fimbriae 2/3, Pertactin (69 kDa protein), Adenylate Cyclase Antigen and B. pertussis Lipopolysaccharide (LPS), all derived from the native B. pertussissource for research and diagnostic purposes. Recombinant Adenylate Cyclase from B. pertussis is now offered in a new, highly purified form, ideal for studies with an active enzyme. Pertussis toxin mutant is a relatively non-toxic protein which may be used in place of the toxin for serology. Additionally, pertussis toxin mutant is a vaccine carrier. These toxins are purified by a tried-and-true method which ensures their activity to high quality standards.

View List Labs Pertussis toxins for sale.

View some of List Labs Pertussis blogs:

By: Suzanne Canada, Ph.D.
Tanager Medical Writing

Pertussis Infections (aka Whooping Cough) Increasing

Rates of pertussis infection, commonly referred to as whooping cough, are on the upswing. Whooping cough is a highly contagious respiratory infection with flu-like symptoms including a blocked or runny nose, sneezing, mild fever and the distinctive, hack-like cough. Prior to the availability of effective whole-cell vaccines, before the mid-1940’s, whooping cough was almost entirely a childhood disease. However, up to half of all cases in the USA are among older children, 7 to 19 years old (CDC Pertussis Surveillance and Reporting, 2013).

Why Are There More Instances of Whooping Cough?

Factors in the resurgence of whooping cough include the level of immunity in a given population, the switch from a whole-cell B. pertussis vaccine to an acellular vaccine (which offered reduced side effects), trends in antigenic variation (e.g., pertactin expression), and the cyclical nature of B. pertussis infections. “Herd immunity” occurs when more than 95% of a given population has up-to-date vaccinations; without this substantial immunized group, outbreaks become more likely, which affect young infants most severely.

Analysis of the genotype profile in strains isolated in Korea in 2011-2012 indicate that genotypic changes in currently circulating strains are strongly associated with the recent increase of pertussis cases (Kim, 2014). One factor in the resurgence may be the rise of pertactin deficient strains of B. pertussis, possibly as an adaptation (Lam 2014).

Whole Cell Vaccines vs. Acellular Vaccines

Previously whole cell vaccines containing chemically-inactivated pertussis cells were the norm, though fever was a known side-effect. Acellular vaccines were introduced in the late 1990’s and have become the standard of care. Acellular vaccines are derived from either three or five key virulence factors from the B. pertussis organism, including pertussis toxin and pertacin. While use of the whole-cell pertussis vaccine resulted in a historic low in 1976 of 1,010 cases reported in the USA, 25,616 new cases of pertussis were reported in 2005, with cyclical incidence rates peaking every 3 to 4 years.

Bordetella Pertussis Used in Research

Bordetella pertussis produces a number of proteins that not only contribute to its pathogenicity, but also are used in research as well (Carbonetti, 2010). The adenylate cyclase toxin (ACT), which is believed to directly penetrate human phagocytes, causes a disruption their normal function by direct production of intracellular cyclic AMP (Kamanova 2008). Pertussis toxin has been used in development of a pertussis diagnosis assay. The recommended pertussis diagnostic tests, culture and real-time PCR assays, lack sensitivity at later stages of the disease. An IgG anti-pertussis toxin ELISA (PT-ELISA) has been introduced as an immunoassay to be used for sero-diagnosis or vaccine evaluation (Kapasi, 2012). Culture and RT-PCR assays detected more cases of pertussis in infants, whereas PT-ELISA detected more cases in adolescents and adults. Serology involving the pertussis toxin is a cost-effective and complementary diagnostic, especially among older children, adolescents, and adults during the late disease phase. More research is required in understanding the long-lasting protective response resulting from vaccination. Pertussis virulence factors from List Biological Laboratories are effective antigens for serology assays.

Pertussis toxin is a protein-based AB₅-type exotoxin with unique qualities that plays a key role in B. pertussis pathogenesis. The exotoxin comprises six subunits (named S1 through S5, where each complex contains two copies of S4) (Kaslow, 1994; Locht, 1995). The subunits are arranged in A-B structure: the A component is enzymatically active and is formed from the S1 subunit, while the B component is the receptor-binding portion and is made up of subunits S2–S5 (Locht, 1995). The subunits are encoded by ptx genes encoded on a large PT operon that also includes additional genes that encode Ptl proteins. Together, these proteins form the PT secretion complex (Weiss, 1993). PT has also become widely used as a biochemical tool to ADP-ribosylate GTP-binding proteins in the study of signal transduction.

List Labs Provides B. Pertussis for Research

List Biological Laboratories provides B. pertussis virulence factors: Pertussis Toxin, Pertussis Toxin Subunits, Filamentous Hemagglutinin (FHA), Fimbriae 2/3, Pertactin (69 kDa protein), Adenylate Cyclase Antigen and B. pertussis Lipopolysaccharide (LPS), all derived from the native B. pertussis source for research and diagnostic purposes. Recombinant Adenylate Cyclase from B. pertussis is now offered in a new, highly purified form, ideal for studies with an active enzyme. Pertussis toxin mutant is a relatively non-toxic protein which may be used in place of the toxin for serology. Additionally, pertussis toxin mutant is a vaccine carrier. These toxins are purified by a tried-and-true method which ensures their activity to high quality standards.

References

CDC Pertussis (Whooping Cough) Surveillance and Reporting: http://www.cdc.gov/pertussis/surv-reporting.html

Carbonetti NH (2010). “Pertussis toxin and adenylate cyclase toxin: key virulence factors of Bordetella pertussis and cell biology tools”. Future Microbiol 5(3): 455–69.

Kamanova J, Kofronova O, Masin J, Genth H, Vojtova J, Linhartova I, Benada O, Just I, Sebo P. (2008) Adenylate cyclase toxin subverts phagocyte function by RhoA inhibition and unproductive ruffling. J Immunol 181(8):5587-97.

Kapasi A, Meade BD, Plikaytis, B, Pawloski L, et al. (2012) Comparative study of different sources of pertussis toxin (PT) as coating antigens in IgG Anti-PT Enzyme-linked immunsobent assays. Clin Vaccine Immunol 19(1):64.

Kaslow HR, Burns DL (June 1992) Pertussis toxin and target eukaryotic cells: binding, entry, and activation FASEB J 6 (9): 2684–90.

Kim SH, Lee J, Sung HY, Yu JY, Kim SH, Park MS, Jung SO (2014) Recent Trends of Antigenic Variation in Bordetella pertussis Isolates in Korea. J Korean Med Sci 29(3):328-33.

Lam C, Octavia S, Ricafort L, Sintchenko V, Gilbert GL, Wood N, et al (2014) Rapid increase in pertactin-deficient Bordetella pertussis isolates, Australia. Emerg Infect Dis 20(4):626-33.

Locht C, Antoine R (1995) A proposed mechanism of ADP-ribosylation catalyzed by the pertussis toxin S1 subunit. Biochimie 77 (5): 333–40.

Weiss A, Johnson F, Burns D (1993) Molecular characterization of an operon required for pertussis toxin secretion Proc Natl Acad Sci USA 90 (7): 2970–4.