John Lennon commemorated by naming a new tarantula species from South America after him

A newly described tarantula species from Western Brazilian Amazonia was named Bumba lennoni in honor of John Lennon, a founder member of the legendary band the Beatles. Credit: Doi: 10.3897/zookeys.448.7920, Image courtesy of Pensoft Publishers

A newly described tarantula species from Western Brazilian Amazonia was named Bumba lennoni in honor of John Lennon, a founder member of the legendary band the Beatles. The new species is part of the tarantula family Theraphosidae which comprises the largest spider species in the world. The study was published in the open access journal ZooKeys.

The name of the new species came across when the authors of the study Fernando Pérez-Miles, from the University of the Republic, Uruguay, and Alexandre Bonaldo and Laura Miglio, both from the Museu Paraense Emilio Goeldi, Brazil, found out that they are all great fans of the Beatles music.

The genus, Bumba, which is proposed as replacement of the old one Maraca, already taken and used for Orthoptera, also has a story behind the choice of name. The new name is taken from Brazilian theatrical folk tradition of the popular festival called Boi-bumbá (hit my bull), which takes place annually in North and Northeastern Brazil.

The new species, as other tarantulas, has defensive urticating hairs on the abdomen which produce irritation upon contact with the skin or sensible tissues.

The specimens used in the study were captured manually or in traps during the night in Caxiuaná, Pará, Brasil, which suggest they could be mainly nocturnal animals.

Source: Pensoft Publishers

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Small, fast, and crowded: Mammal traits amplify tick-borne illness

Chipmunks are small-bodied animals with fast lives and dense populations. When ticks feed on them, they are more likely to pick up multiple disease-causing pathogens. Credit: © dwags / Fotolia

In the U.S., some 300,000 people are diagnosed with Lyme disease annually. Thousands also suffer from babesiosis and anaplasmosis, tick-borne ailments that can occur alone or as co-infections with Lyme disease. According to a new paper published in PLOS ONE, when small, fast-living mammals abound, so too does our risk of getting sick.

In eastern and central North America, blacklegged ticks are the primary vectors for Lyme disease, babesiosis, and anaplasmosis. The pathogens that cause these illnesses are widespread in nature; ticks acquire them when they feed on infected animals.

Richard S. Ostfeld, the paper's lead author and a scientist at the Cary Institute of Ecosystem Studies, has researched the ecology of Lyme disease since 1992. "A pattern emerged in our long-term studies. Ticks that fed on certain rodents and shrews were much more likely to pick up multiple pathogens, making the environment riskier for people."

To investigate why mammals differ in their 'reservoir competence' or ability to transmit pathogens to ticks, Ostfeld and his co-authors from Bard College, Oregon State University, the University of South Florida, and EcoHealth Alliance took a two-pronged approach.

First, they looked at life history traits for nine mammals known to harbor Lyme disease, babesiosis, and anaplasmosis. Attributes like body size, litter size, and life span were taken into consideration.

Then they looked at the role of mammal population density. As 'sit and wait' parasites, ticks are much more likely to encounter animals with dense populations. This, in turn, could help pathogens evolve to exploit specific hosts, resulting in more effective transmission rates.

For Lyme disease and anaplasmosis, fast life history features were a strong predictor of an animal's ability to transmit infection to ticks. Body size was inversely related to reservoir competence. Raccoon, skunk, opossum, squirrel, and deer infected fewer ticks than their mouse, chipmunk, and shrew counterparts.

Ostfeld notes, "This is consistent with past research on Lyme disease, West Nile virus, and Eastern Equine encephalitis. There is evidence that animals that mature early and have frequent, large litters invest less in some immune defenses, making them better pathogen hosts."

Population density was the best predictor of species' abilities to transmit all three pathogen groups, with animals that ticks encountered most frequently being the most effective at transferring infection. Co-author Felicia Keesing of Bard College explains, "Fast life history and high population density often go hand-in-hand. In rodents and shrews, pathogen adaptation and poor immune defense may be working together to amplify disease spread."

With Ostfeld concluding, "In our struggle to manage the ever-growing list of tick-borne diseases, we need to understand which animals magnify human disease risk. Our results suggest when generalist pathogens emerge, small mammals with large populations and a fast pace of life warrant careful monitoring."

Source: Cary Institute of Ecosystem Studies

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How spiders spin silk: Mechanism elegantly explains how spider silk can form so quickly and smoothly

Spider silk is an impressive material; lightweight and stretchy yet stronger than steel. But the challenge that spiders face to produce this substance is even more formidable. Credit: © Tamas Zsebok / Fotolia

Spider silk is an impressive material; lightweight and stretchy yet stronger than steel. But the challenge that spiders face to produce this substance is even more formidable. Silk proteins, called spidroins, must convert from a soluble form to solid fibers at ambient temperatures, with water as a solvent, and at high speed. How do spiders achieve this astounding feat? In new research publishing in the open access journal PLOS Biology on August 5, Anna Rising and Jan Johansson show how the silk formation process is regulated. The work was done at the Swedish University of Agricultural Sciences (SLU) and Karolinska Institutet in collaboration with colleagues in Latvia, China and USA.

Spidroins are big proteins of up to 3,500 amino acids that contain mostly repetitive sequences, but the most important bits for the conversion of spidroins into silk are the ends. 

These terminal regions of the proteins are unique to spider silk and are very similar between different spiders. Spidroins have a helical and unordered structure when stored as soluble proteins in silk glands, but when converted to silk their structure changes completely to one that confers a high degree of mechanical stability. These changes are triggered by an acidity (pH) gradient present between one end of the spider silk gland and the other. The gland proceeds from a narrow tail to a sac to a slender duct, and it is known that silk forms at a precise site within the duct. However, further details of spider silk production have been elusive.

By using highly selective microelectrodes to measure the pH within the glands, the authors showed the pH falls from a neutral pH of 7.6 to an acidic pH of 5.7 between the beginning of the tail and half-way down the duct, and that the pH gradient was much steeper than previously thought. The microelectrodes also showed that the concentration of bicarbonate ions and pressure of carbon dioxide simultaneously rise along the gland. Taken together, these patterns suggested that the pH gradient might form through the action of an enzyme called carbonic anhydrase, which converts carbon dioxide and water to bicarbonate and hydrogen ions (and thereby creating an acidic environment). Using a method developed by the authors, they were able to identify active carbonic anhydrase in the narrower part of the gland and confirm that carbonic anhydrase is indeed responsible for generating the pH gradient.

The authors also found that pH had opposite effects on the stability of the two regions at each end of the spidroin proteins, which was surprising given that these regions had been suggested to have similar roles in silk formation. While one of the ends (the "N-terminal domain") tended to pair up with other molecules at the beginning of the duct and became increasingly stable as the acidity increased along the duct, the other end (the "C-terminal domain") destabilized as the acidity increased, and gradually unfolded until it formed the structure characteristic of silk at the acidic pH of 5.5. These findings show that both ends of the protein undergo dramatic structural changes at the pH found at the beginning of the duct, which is also the point where carbonic anhydrase activity is concentrated.

These insights led the authors to propose a new "lock and trigger" model for spider silk formation, in which gradual pairing up of the N-terminal domains locks spidroins into a network of many protein molecules, while the changes of structure in the C-terminal domains could trigger the rapid polymerization of spidroins into fibers. Interestingly, the structure of the C-terminal domain is similar to those in the "amyloid" fibrils found in the brains of individuals with diseases such as Alzheimer's disease. This mechanism elegantly explains how spider silk can form so quickly and smoothly within the spinning duct of these amazing animals. Besides helping humans to understand how they might mimic the spiders to produce biomimetic spidroin fibers for our own purposes, knowing how spiders spin silk could give insights into natural ways of hindering the amyloid fibrils associated with diseases like dementia.

Source: PLOS

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Physicians seeing increase in brown recluse spider bites

The brown recluse spider has a violin-shaped marking on its back. Credit: CDC image library

Vanderbilt medical toxicologists are reporting an increase in patients seen with brown recluse spider bites this summer.

The venomous bites usually heal well if left alone, according to Tennessee Poison Center Medical Director Donna Seger, M.D., but there are so many urban legends about these bites, patients frequently apply many treatments before seeking medical advice.

There are two components to spider bites -- the cutaneous lesion and, more rarely, the systemic symptoms that can occur following the bite. The syndrome known as systemic loxsoscelism consists of brown recluse spider bites accompanied by a fever, rash, muscle pain, with or without hemolysis (breaking down of red blood cells), which can be life threatening, especially in children, Seger said.

"Our recommendations are that all children under 12 with a brown recluse spider bite should have a urine test for the presence of hemoglobin in blood which indicates hemolysis," Seger said.

"If the urine is positive for blood and/or the child has other signs of systemic loxsoscelism (rash, fever), the child should be admitted and observed for hemolysis. If the urine dip is negative, and there are no other signs of systemic loxsoscelism, the child should be seen by a physician the next day."

If adults with a brown recluse spider bite do not have rash, fever or muscle pain there is no need to do a urine test, Seger said.

"As physicians, it is hard for us to do nothing. The cutaneous lesion has classic characteristics, but if physicians are not familiar with this bite, the tendency is to debride and cut out the lesion. This actually slows the healing process and can result in disfigurement that would not occur if the lesion were left alone. Ointments, antibiotics, and dapsone are not recommended. Ice works better than opiates for pain," Seger said.

"We don't know why systemic loxsoscelism occurs in some people with a brown recluse spider bite and not in others but it is life-threatening and does require immediate medical attention. Toxin-induced hemolysis can occur very rapidly and therein lies the life threat, especially in children."

The brown recluse spider, also known as the violin spider, is usually between 6-20 mm. It is typically light to medium brown but can range in color from cream-colored to dark brown or blackish gray. It has six eyes instead of eight and can be identified by the violin-shaped marking on its back.

Source: Vanderbilt University Medical Center

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