Same-sex pathogen mating caused Vancouver Island outbreak; Atoms almost at a standstill; How does kinesin know to go forward?; Kinesin twist; Fluorescent gonads speed mosquito control; Alzheimer's disease - understanding the lipid connection.

NATURE AND THE NATURE RESEARCH JOURNALS PRESS RELEASE. For papers that will be published online on 9 October 2005


For papers that will be published online on 9 October 2005

This press release contains:
* Same-sex pathogen mating caused Vancouver Island outbreak - Nature
* Atoms almost at a standstill - Nature Physics
* How does kinesin know to go forward? - Nature Chemical Biology
* Kinesin twist - Nature Chemical Biology
* Fluorescent gonads speed mosquito control - Nature Biolotechnology
* Alzheimer's disease - understanding the lipid connection - Nature Cell Biology
* Mention of papers to be published at the same time with the same embargo
* Geographical listing of authors

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[1] Same-sex pathogen mating caused Vancouver Island outbreak

DOI: 10.1038/nature04220

Geneticists have unravelled the story behind the emergence of a virulent
strain of fungus that caused a 1999 outbreak of meningoencephalitis on
Vancouver Island, Canada. Two strains - one local one found in the Pacific
Northwest, and another that had migrated from Australia - combined through
sexual reproduction, despite the fact that both were of the same 'sex'.
Strains of the fungi species in question, Cryptococcus gattii, typically
belong to one of two sexual groups, called 'a' and 'alpha', explain Joseph
Heitman and his colleagues in a paper published online this week by Nature.
Usually, sexual reproduction occurs between different sexual groups, but
analysis of the fungus that caused the 1999 outbreak shows that this
disease-causing strain is descended from two alpha strains.
It remains to be seen whether such mating is a common occurrence in the
wild, and whether this particular event facilitated the production of fungal
spores, the particles that actually infect humans. The authors add that
same-sex mating might also be common in other parasites, such as
Trypanosoma, Leishmania and the malaria-causing Plasmodium falciparum.

Author contact:
Joseph Heitman (Duke University Medical Center, HHMI, Durham, NC, USA)
Tel: +1 919 684 2824, E-mail: [email protected]

************************NATURE PHYSICS***************************

[2] Atoms almost at a standstill

DOI: 10.1038/nphys120

Using laser beams and a trap made from mirrors, Gerhard Rempe and colleagues
can catch single atoms and cool them down to the point at which they nearly
stand still. As they report in Nature Physics, using this technique they can
trap a well-controlled number of atoms for tens of seconds - which is very
long compared with the trapping times of fractions of a second that have so
far defined the state of the art. This advance could prove important for the
further exploration of how atoms and molecules behave in the quantum world.
These experiments constitute the latest progress in what is known as 'cavity
quantum electrodynamics', concerning the trapping of particles in tiny
cavities between two highly reflecting mirrors. Such settings enable
exquisite control over the interactions between light and matter at the
level of single atoms and single photons. The long trapping times now
realized mean that, for practical purposes, single atoms can be permanently
confined to the cavity - an attractive property with regard to exploiting
few-atom systems for fundamental studies and for applications.

Author contact:
Gerhard Rempe (Max-Planck-Institut fur Quantenoptik, Garching, Germany)
Tel: +49 89 32905 701, E-mail: [email protected]

Other papers from Nature Physics to be published online at the same time and
with the same embargo:

[3] Anomalous field-induced particle orientation in dilute mixtures of
charged rod-like and spherical colloids
DOI: 10.1038/nphys124

*******************NATURE CHEMICAL BIOLOGY*********************

[4] How does kinesin know to go forward?

DOI: 10.1038/nchembio741

Entropy drives kinesin forward according to a paper in the November issue of
Nature Chemical Biology. Kinesin is a protein that walks-one foot after
another-along microtubules delivering vesicle cargo around the cell.
Although much is known about how kinesin moves, no one knew exactly what
made kinesin walk forward instead of backward.
To address this question, Toshio Yanagida and colleagues used a
technique called 'optical tweezers', in which microscopic beads are attached
to individual kinesin proteins. Light from a laser beam is used to capture
the bead in an 'optical trap' and move the bead and protein around. Using
this single-molecule technique, the authors looked at the effects of
different forces and temperatures on kinesin walking forward and backward
(kinesin can be made to walk backwards by pushing on it with the optical
tweezers). These results showed that it is entropy that drives kinesin
forward, probably because a forward step along the microtubule is a better
'fit' than a backward step.
Besides increasing our understanding of how kinesin marches around
cells, the results of Yanagida and coworkers may be more broadly applicable,
explaining how other proteins know where to go along the cytoskeleton-the
roadways of a cell.

Author contact:
Toshio Yanagida (Osaka University, Osaka, Japan)
Tel: +81 6 6879 4630, E-mail: [email protected]

[5] Kinesin twist

DOI: 10.1038/nchembio740

In the November issue of Nature Chemical Biology, a paper reports that
kinesin rotates microtubules sideways while it moves forward. Kinesin is a
protein that walks-one foot after another-along microtubules in order to
move vesicles around the inside of cells. Before this report, scientists
generally believed that kinesin moved forward without any side-to-side
Cross and colleagues used microscopy to watch kinesin moving along
microtubules. They fitted the microtubules with an arm that stuck out to the
side to observe if kinesin motion caused any rotation in the microtubules.
Surprisingly, they found that microtubules rotated counterclockwise. In
addition, they found that this motion was driven by ATP consumption.
This newly found torque force of kinesin suggests that additional
protein-protein interactions could be involved as kinesin walks along, and
it should stimulate new efforts to understand the molecular details of this

Author contact:
Robert A. Cross (Marie Curie Research Institute, Oxted, UK)
Tel: +44 1883 722 306, E-mail: [email protected]

********************NATURE BIOTECHNOLOGY*********************

[6] Fluorescent gonads speed mosquito control

DOI: 10.1038/nbt1152

Researchers have found a reliable way of rapidly identifying sterile male
mosquitoes for use in pest eradication programs for controlling malaria. In
the November issue of Nature Biotechnology, Andrea Crisanti and colleagues
establish a genetic approach for identifying male larvae of the malaria
vector mosquito Anopheles stephensi through the specific expression of a
green fluorescent protein in their gonads. By releasing an overabundance of
these sterile males in the field, wild male mosquitoes would be unable to
mate with females, leading to rapid decline in fertile eggs and the eventual
eradication of the mosquito population in the area of release.
The sexing strategy described by Crisanti and colleagues solves the
longstanding problem of how to differentiate female sterile mosquitoes,
which remain vectors for parasites of the genus Plasmodium that cause
malaria and are thus unsuitable for use in pest control from sterile males
that do not transmit the parasites. Previously, the precise sorting of males
from females among the sterilized larvae was practically impossible. By
ensuring that expression of the fluorescent protein occurs only when male
gonads appear in mosquito larvae, the authors are able to sort the
translucent larvae into female and male on the basis of their fluorescence
using existing cell sorting technologies. The sexing of the malaria vector
A. stephensi brings this type of mosquito control several steps closer to
practical implementation.

Author contact:
Andrea Crisanti (Imperial College London, UK)
Tel: +44 207 5945412, E-mail: [email protected]

Additional contact for comment on paper:
Peter W. Atkinson (University of California, Riverside, CA, USA)
Tel: +1 951 827 4782, E-mail: [email protected]

Other papers from Nature Biotechnology to be published online at the same
time and with the same embargo:

[7] Efficient in vivo gene expression by trans-splicing adeno-associated
viral vectors
DOI: 10.1038/nbt1153

**********************NATURE CELL BIOLOGY***********************

[8] Alzheimer's disease - understanding the lipid connection

DOI: 10.1038/ncb1313

Keeping an eye on cholesterol can reduce the risk of heart disease and
stroke but new research shows how it may also have benefits for warding off
Alzheimer's disease. The function of a mysterious protein, how it affects
Alzheimer's and its link to cholesterol is reported in the November issue of
the Nature Cell Biology.
Studies suggest that high cholesterol levels can be linked with increasing
levels of a protein called amyloid-beta (AB). Accumulation of this protein
is a central feature of Alzheimer's and thought to lead to the neuronal
dysfunction and death associated with Alzheimer's. Produced in normal cells,
AB comes from a larger protein called amyloid precursor protein (APP). The
normal function of both remains a mystery but AB's levels increase sharply
in Alzheimer's.
Tobias Hartmann and colleagues examined whether APP and AB could affect
lipid metabolism. Cells derived from mice, engineered to remove expression
of the enzymes that generate AB had higher levels of cholesterol and of
another lipid called sphingomyelin. The team pinpointed these effects to
altered activities of two key enzymes in the metabolic pathways of these
lipids. They also restored normal levels of these lipids and the enzyme
activities by treating these cells with AB. The authors concluded that one
function of normal APP is in lipid metabolism - a surprising finding. This
study also suggest the existence of a loop - AB levels are controlled by
lipids and lipids, in turn, control AB levels - so, such a spiralling
mechanism could result in the abnormally high AB levels seen in Alzheimer's,
having clear consequences for designing therapeutic interventions.

Author contact:
Tobias Hartmann (University of Heidelberg, Germany)
Tel: +49 6221 546844, E-mail: [email protected]

Other papers from Nature Cell Biology to be published online at the same
time and with the same embargo:

[9] Recruitment of MLL by HMG-domain protein iBRAF promotes neural
DOI: 10.1038/ncb1312


Items from other Nature journals to be published online at the same time and
with the same embargo:


[10] Blue-light emission at room temperature from Ar+ -irradiated SrTiO3
DOI: 10.1038/nmat1498

[11] Flux crystal growth and thermal stabilities of LiV2O4
DOI: 10.1038/nmat1499

[12] High-efficiency solution processable polymer photovoltaic cells by
self-organization of polymer blends
DOI: 10.1038/nmat1500

Nature MEDICINE (<>)

[13] CCL5-CCR5 interaction provides antiapoptotic signals for macrophage
survival during viral infection
DOI: 10.1038/nm1303

[14] NKCC1 transporter facilitates seizures in the developing brain
DOI: 10.1038/nm1301


[15] Population structure, differential bias and genomic control in a
large-scale, case-control association study
DOI: 10.1038/ng1653

[16] Genetic variation in selenoprotein S influences inflammatory response
DOI: 10.1038/ng1655

[17] Monovalent cation leaks in human red cells caused by single amino-acid
substitutions in the transport domain of the band 3 chloride-bicarbonate
exchanger, AE1
DOI: 10.1038/ng1656


[18] Fine-scale specificity of cortical networks depends on inhibitory cell
type and connectivity
DOI: 10.1038/nn1565

[19] TARP gamma-8 controls hippocampal AMPA receptor number, distribution
and synaptic plasticity
DOI: 10.1038/nn1551

Nature IMMUNOLOGY (<>)

[20] N-Acetylglucosamine-6-O-sulfotransferases 1 and 2 cooperatively control
lymphocyte homing through L-selectin ligand biosynthesis in high endothelial
DOI: 10.1038/ni1259

[21] A major class of L-selectin ligands is eliminated in mice deficient in
two sulfotransferases expressed in high endothelial venules
DOI: 10.1038/ni1258


[22] Cbl promotes clustering of endocytic adaptor proteins
DOI: 10.1038/nsmb1000

[23] A minimal domain responsible for Munc13 activity
DOI: 10.1038/nsmb1001

[24] New catalytic structures from an existing ribozyme
DOI: 10.1038/nsmb1003

[25] Dual modes of RNA-silencing suppression by Flock House virus protein B2

DOI: 10.1038/nsmb1005


The following list of places refers to the whereabouts of authors on the
papers numbered in this release. The listing may be for an author's main
affiliation, or for a place where they are working temporarily. Please see
the PDF of the paper for full details.

Caulfield: 16
Waurn Ponds: 16

Leuven: 8

Grenoble: 9
Nice: 17
Paris: 19

Frankfurt: 22
Garching near Munich: 2
Heidelberg: 8, 22

Monza: 3
Naples: 17
Segrate: 3

Ikoma: 10
Kashiwa: 11
Kyoto: 4, 10
Matsumoto: 20
Nagoya: 18, 20, 21
Shizuoka: 10
Suita: 4
Toyonaka: 4

Madrid: 22

Villigen: 13
Zurich: 17

Oxted: 5
Cambridge: 15
Bristol: 17
Oxford: 17
London: 6, 17, 22

La Jolla: 18, 20, 25
Los Angeles: 12
San Francisco: 19, 21
South San Francisco: 15
Denver: 14
Golden: 14
Iowa City: 7
Bethesda: 19
Boston: 8, 14, 21
Cambridge: 24
Ann Arbor: 20
Columbia: 7
St. Louis: 9, 13
North Carolina
Durham: 1, 13
Philadelphia: 9, 13
Nashville: 14
Dallas: 23
Houston: 23
San Antonio: 16
Seattle: 7
Milwaukee: 16


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Katharine Mansell (Nature London)
Tel: +44 20 7843 4658; E-mail: [email protected]

For media inquiries relating to editorial content/policy for the Nature
Research Journals, please contact the journals individually:

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Kathy Aschheim
Tel: +1 212 726 9346; E-mail: [email protected]

Nature Cell Biology (London)
Bernd Pulverer
Tel: +44 20 7843 4892; E-mail: [email protected]
Nature Chemical Biology (Boston)
Beatrice Chrystall
Tel: +1 617 475 9241, E-mail: [email protected]

Nature Genetics (New York)
Orli Bahcall
Tel: +1 212 726 9311; E-mail: [email protected]

Nature Immunology (New York)
Laurie Dempsey
Tel: +1 212 726 9372; E-mail: [email protected]

Nature Materials (London)
Maria Bellantone
Tel: +44 20 7843 4556; E-mail: [email protected]

Nature Medicine (New York)
Juan Carlos Lopez
Tel: +1 212 726 9325; E-mail: [email protected]

Nature Neuroscience (New York)
Sandra Aamodt (based in California)
Tel: +1 530 795 3256; E-mail: [email protected]

Nature Structural & Molecular Biology (New York)
Ed Feng
Tel: +1 212 726 9351; E-mail: [email protected]

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Published: 09 Oct 2005

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